304:, protein folding, and cell wall synthesis. The initial contact between the peptide and the target organism is electrostatic, as most bacterial surfaces are anionic, or hydrophobic, such as in the antimicrobial peptide Piscidin. Their amino acid composition, amphipathicity, cationic charge and size allow them to attach to and insert into membrane bilayers to form pores by ‘barrel-stave’, ‘carpet’ or ‘toroidal-pore’ mechanisms. Alternately, they may penetrate into the cell to bind intracellular molecules which are crucial to cell living. Intracellular binding models includes inhibition of cell wall synthesis, alteration of the cytoplasmic membrane, activation of autolysin, inhibition of DNA, RNA, and protein synthesis, and inhibition of certain enzymes. In many cases, the exact mechanism of killing is not known. One emerging technique for the study of such mechanisms is
730:
104:
141:
residues aligned along one side and hydrophobic amino acid residues aligned along the opposite side of a helical molecule. This amphipathicity of the antimicrobial peptides allows them to partition into the membrane lipid bilayer. The ability to associate with membranes is a definitive feature of antimicrobial peptides, although membrane permeabilization is not necessary. These peptides have a variety of antimicrobial activities ranging from membrane permeabilization to action on a range of cytoplasmic targets.
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402:
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33:
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calculation interface. It also provides links to many other tools. CAMP contains AMP prediction, feature calculator, BLAST search, ClustalW, VAST, PRATT, Helical wheel etc. In addition, ADAM allows users to search or browse through AMP sequence-structure relationships. Antimicrobial peptides often encompass a wide range of categories such as antifungal, antibacterial, and antituberculosis peptides.
349:
functions in vivo (e.g. hepcidin). Dusquetide for example is an immunomodulator that acts through p62, a protein involved in toll like receptor based signalling of infection. The peptide is being examined in a Phase III clinical trial by
Soligenix (SGNX) to ascertain if it can assist in repair of radiation-induced damage to oral mucosa arising during cancer radiotherapy of the head and neck.
1083:). Based on the APD, other databases have also been built, including ADAM (A Database of Anti-Microbial peptides), BioPD (Biologically active Peptide Database), CAMP (Collection of sequences and structures of antimicrobial peptides), DBAASP (Database of Antimicrobial Activity and Structure of Peptides), DRAMP (Data Repository of Antimicrobial Peptides)
707:); and the presence of these cholesterols will also generally reduce the activities of the antimicrobial peptides, due either to stabilization of the lipid bilayer or to interactions between cholesterol and the peptide. So the cholesterol in mammalian cells will protect the cells from attack by the antimicrobial peptides.
797:
and fluorinated amino acids in the hydrophobic phase are believed to break the secondary structure and thus reduce hydrophobic interaction with mammalian cells. It has also been found that Pro→Nlys substitution in Pro-containing β-turn antimicrobial peptides was a promising strategy for the design of
610:
AMPs have been observed having functions other than bacterial and fungal killing. These activities include antiviral effects, but also roles in host defence such as anticancer functions and roles in neurology. This has led to a movement for re-branding AMPs as "Host-defence peptides" to encompass the
908:
The ‘Trojan Horse’ approach to solving this problem capitalizes on the innate need for iron by pathogens. “Smuggling” antimicrobials into the pathogen is accomplished by linking them to siderophores for transport. While simple in concept, it has taken many decades of work to accomplish the difficult
392:
Disordered toroidal-pore model: According to this model, the disordered AMPs wrap around the lipid bilayer and create a pore, which disrupts the membrane's integrity and leads to the death of the microbe. Unlike the toroidal model, which suggests that the AMP creates a stable toroidal structure, the
388:
Toroidal model: The toroidal model proposes that AMPs interact with the lipid bilayer of the microbial cell membrane to form toroidal structures, which are thought to pinch off sections of the membrane and lead to the formation of vesicles. This process is thought to disrupt the membrane's integrity
384:
Carpet model: The carpet model proposes that AMPs adsorb onto the lipid bilayer of the microbial cell membrane, forming a dense layer that causes the membrane to become permeabilized. This model suggests that the AMP acts as a "carpet" that covers the surface of the cell, preventing the microbe from
140:
or loop due to the presence of a single disulfide bond and/or cyclization of the peptide chain, and iv) extended. Many of these peptides are unstructured in free solution, and fold into their final configuration upon partitioning into biological membranes. The peptides contain hydrophilic amino acid
111:
Antimicrobial peptides are a unique and diverse group of molecules, which are divided into subgroups on the basis of their amino acid composition and structure. Antimicrobial peptides are generally between 12 and 50 amino acids. These peptides include two or more positively charged residues provided
2888:
Arockiaraj J, Chaurasia MK, Kumaresan V, Palanisamy R, Harikrishnan R, Pasupuleti M, Kasi M (April 2015). "Macrobrachium rosenbergii mannose binding lectin: synthesis of MrMBL-N20 and MrMBL-C16 peptides and their antimicrobial characterization, bioinformatics and relative gene expression analysis".
904:
While these examples show that resistance can evolve naturally, there is increasing concern that using pharmaceutical copies of antimicrobial peptides can make resistance happen more often and faster. In some cases, resistance to these peptides used as a pharmaceutical to treat medical problems can
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Some cecropins (e.g. cecropin A, and cecropin B) have anticancer properties and are called anticancer peptides (ACPs). Hybrid ACPs based on
Cecropin A have been studied for anticancer properties. The fruit fly Defensin prevents tumour growth, suspected to bind to tumour cells owing to cell membrane
432:
through interactions with specific phospholipids. From the computational point of view, Molecular
Dynamics simulations can provide detailed information about the structure and dynamics of the peptide-membrane interactions, including the orientation, conformation, and insertion of the peptide in the
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species reduce the fluidity of their outer membrane by increasing hydrophobic interactions between an increased number of Lipid A acyl tails by adding myristate to Lipid A with 2-hydroxymyristate and forming hepta-acylated Lipid A by adding palmitate. The increased hydrophobic moment is thought to
375:
Antimicrobial peptides generally have a net positive charge, allowing them to interact with the negatively charged molecules exposed on bacteria and cancer cell surfaces, such as phospholipid phosphatidylserine, O-glycosylated mucins, sialylated gangliosides, and heparin sulfates. The mechanism of
348:
and cells of the adaptive immune response. Animal models indicate that host defense peptides are crucial for both prevention and clearance of infection. It appears as though many peptides initially isolated as and termed "antimicrobial peptides" have been shown to have more significant alternative
714:
is well known to affect peptide-lipid interactions. There's an inside-negative transmembrane potential existing from the outer leaflet to the inner leaflet of the cell membranes and this inside-negative transmembrane potential will facilitate membrane permeabilization probably by facilitating the
319:
AMPs can possess multiple activities including anti-gram-positive bacterial, anti-gram-negative bacterial, anti-fungal, anti-viral, anti-parasitic, and anti cancer activities. A big AMP functional analysis indicates that among all AMP activities, amphipathicity and charge, two major properties of
757:
In contrast, the outer part of the membranes of plants and mammals is mainly composed of lipids without any net charges since most of the lipids with negatively charged headgroups are principally sequestered into the inner leaflet of the plasma membranes. Thus in the case of mammalian cells, the
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dbAMP: Provides an online platform for exploring antimicrobial peptides with functional activities and physicochemical properties on transcriptome and proteome data. dbAMP is an online resource that addresses various topics such as annotations of antimicrobial peptides (AMPs) including sequence
884:
Outer membrane vesicles produced by Gram-negative bacteria bind the antimicrobial peptides and sequester them away from the cells, thereby protecting the cells. The outer membrane vesicles are also known to contain various proteases, peptidases and other lytic enzymes, which may have a role in
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The
Antimicrobial peptide databases may be divided into two categories on the basis of the source of peptides it contains, as specific databases and general databases. These databases have various tools for antimicrobial peptides analysis and prediction. For example, the APD has a widely used
693:
There are some factors that are closely related to the selectivity property of antimicrobial peptides, among which the cationic property contributes most. Since the surface of the bacterial membranes is more negatively charged than mammalian cells, antimicrobial peptides will show different
673:
In the competition of bacterial cells and host cells with the antimicrobial peptides, antimicrobial peptides will preferentially interact with the bacterial cell to the mammalian cells, which enables them to kill microorganisms without being significantly toxic to mammalian cells.
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retard or abolish antimicrobial peptide insertion and pore formation. The residues undergo alteration in membrane proteins. In some Gram-negative bacteria, alteration in the production of outer membrane proteins correlates with resistance to killing by antimicrobial peptides.
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insertion of positively charged peptides into membranes. By comparison, the transmembrane potential of bacterial cells is more negative than that of normal mammalian cells, so bacterial membrane will be prone to be attacked by the positively charged antimicrobial peptides.
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Barrel-stave model: The barrel-stave model proposes that AMPs interact with the lipid bilayer of the microbial cell membrane to form transmembrane channels or "barrel staves". These channels are thought to disrupt the membrane's integrity, leading to the death of the
653:) without off-target cytotoxicity. The multi-target mechanism of action involves outer membrane permeabilization followed by biofilm disruption triggered by the inhibition of efflux pump activity and interactions with extracellular and intracellular nucleic acids.
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hurdle of transporting antimicrobials across the cell membranes of pathogens. Lessons learned from the successes and failures of siderophore-conjugate drugs evaluated during the development of novel agents using the ‘Trojan horse’ approach have been reviewed.
533:
Antimicrobial peptides have been used as therapeutic agents; their use is generally limited to intravenous administration or topical applications due to their short half-lives. As of
January 2018 the following antimicrobial peptides were in clinical use:
770:. Therefore, the hydrophobic interaction between the hydrophobic face of amphipathic antimicrobial peptides and the zwitterionic phospholipids on the cell surface of mammalian cell membranes plays a major role in the formation of peptide-cell binding.
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information, antimicrobial activities, post-translational modifications (PTMs), structural visualization, antimicrobial potency, target species with minimum inhibitory concentration (MIC), physicochemical properties, or AMP–protein interactions.
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action of these peptides varies widely but can be simplified into two categories: membranolytic and non-membranolytic antimicrobial peptides. The disruption of membranes by membranolytic antimicrobial peptides can be described by four models:
320:
AMPs, best distinguish between AMPs with and without anti-gram-negative bacterial activities. This implies that being AMPs with anti-gram-negative bacterial activities may prefer or even require strong amphipathicity and net positive charge.
3783:
Kulkarni HM, Swamy C, Jagannadham MV (March 2014). "Molecular characterization and functional analysis of outer membrane vesicles from the antarctic bacterium
Pseudomonas syringae suggest a possible response to environmental conditions".
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rupture membranes by identifying key phospholipids in the cell membranes of the pathogen. Human defensins have been thought to act through a similar mechanism, targeting cell membrane lipids as part of their function. In fact human
3429:
Zhu WL, Lan H, Park Y, Yang ST, Kim JI, Park IS, et al. (October 2006). "Effects of Pro → peptoid residue substitution on cell selectivity and mechanism of antibacterial action of tritrpticin-amide antimicrobial peptide".
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A lot of effort has been put into controlling cell selectivity. For example, attempts have been made to modify and optimize the physicochemical parameters of the peptides to control the selectivities, including net charge,
877:
ATP-binding cassette transporters import antimicrobial peptides and the resistance-nodulation cell-division efflux pump exports antimicrobial peptides. Both transporters have been associated with antimicrobial peptide
2809:
Kumaresan V, Bhatt P, Ganesh MR, Harikrishnan R, Arasu M, Al-Dhabi NA, et al. (December 2015). "A novel antimicrobial peptide derived from fish goose type lysozyme disrupts the membrane of
Salmonella enterica".
1921:"Dusquetide: A novel innate defense regulator demonstrating a significant and consistent reduction in the duration of oral mucositis in preclinical data and a randomized, placebo-controlled phase 2a clinical study"
287:
The modes of action by which antimicrobial peptides kill microbes are varied, and may differ for different bacterial species. Some antimicrobial peptides kill both bacteria and fungi, e.g., psoriasin kills
316:. In general the antimicrobial activity of these peptides is determined by measuring the minimal inhibitory concentration (MIC), which is the lowest concentration of drug that inhibits bacterial growth.
1714:
Hirst DJ, Lee TH, Swann MJ, Unabia S, Park Y, Hahm KS, Aguilar MI (April 2011). "Effect of acyl chain structure and bilayer phase state on binding and penetration of a supported lipid bilayer by HPA3".
3968:
Gumienna-Kontecka E, Carver PL (2019). "Chapter 7. Building a Trojan Horse: Siderophore-Drug
Conjugates for the Treatment of Infectious Diseases". In Sigel A, Freisinger E, Sigel RK, Carver PL (eds.).
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Arasu A, Kumaresan V, Ganesh MR, Pasupuleti M, Arasu MV, Al-Dhabi NA, Arockiaraj J (June 2017). "Bactericidal activity of fish galectin 4 derived membrane-binding peptide tagged with oligotryptophan".
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Tools such as
PeptideRanker, PeptideLocator, and AntiMPmod allow for the prediction of antimicrobial peptides while others have been developed to predict antifungal and anti-Tuberculosis activities.
1564:
O'Driscoll NH, Labovitiadi O, Cushnie TP, Matthews KH, Mercer DK, Lamb AJ (March 2013). "Production and evaluation of an antimicrobial peptide-containing wafer formulation for topical application".
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Chou HT, Kuo TY, Chiang JC, Pei MJ, Yang WT, Yu HC, et al. (August 2008). "Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp".
2766:
Hassan M, Kjos M, Nes IF, Diep DB, Lotfipour F (October 2012). "Natural antimicrobial peptides from bacteria: characteristics and potential applications to fight against antibiotic resistance".
2444:
Gomes B, Augusto MT, Felício MR, Hollmann A, Franco OL, Gonçalves S, Santos NC (9 January 2018). "Designing improved active peptides for therapeutic approaches against infectious diseases".
83:
bacteria, enveloped viruses, fungi and even transformed or cancerous cells. Unlike the majority of conventional antibiotics it appears that antimicrobial peptides frequently destabilize
685:, and in some cases, they are reported to be more resistant than the surrounding normal cells. Therefore, we cannot conclude that selectivity is always high against cancer cells.
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5190:
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Ageitos JM, Sánchez-Pérez A, Calo-Mata P, Villa TG (June 2017). "Antimicrobial peptides (AMPs): Ancient compounds that represent novel weapons in the fight against bacteria".
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infected by GFP-producing bacteria. Red-eyed flies lacking antimicrobial peptide genes are susceptible to infection, while white-eyed flies have a wild-type immune response.
793:, hydrophobicity per residue (H), hydrophobic moment (μ) and the angle subtended by the positively charged polar helix face (Φ). Other mechanisms like the introduction of D-
2926:
3744:"The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases"
3380:
Lee TH, Hall K, Mechler A, Martin L, Popplewell J, Ronan G, Aguilar MI (2009). "Molecular
Imaging and Orientational Changes of Antimicrobial Peptides in Membranes".
107:
Antimicrobial peptides from animals, plants and fungi organised by their secondary structure content. Circle size indicates overall molecular weight of each peptide.
498:
to measure the secondary structure, orientation and penetration of antimicrobial peptides into lipid bilayers in the biologically relevant liquid-crystalline state
1480:
Varkey J, Singh S, Nagaraj R (November 2006). "Antibacterial activity of linear peptides spanning the carboxy-terminal beta-sheet domain of arthropod defensins".
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is normally widely distributed in the mammalian cell membranes as a membrane stabilizing agent but absent in bacterial cell membranes (except when sequestered by
4447:"dbAMP: an integrated resource for exploring antimicrobial peptides with functional activities and physicochemical properties on transcriptome and proteome data"
722:, which in general reduces the activity of most antimicrobial peptides, contributes partially to the selectivity of the antimicrobial peptides by weakening the
874:
remodels its membranes to make it appear as if the bacterium has already been successfully attacked by AMPs, protecting it from being attacked by more AMPs.
3345:
Yu L, Guo L, Ding JL, Ho B, Feng SS, Popplewell J, et al. (February 2009). "Interaction of an artificial antimicrobial peptide with lipid membranes".
2953:
4919:
Python package for computational work with antimicrobial peptides, including sequence handling, -design, -prediction, descriptor calculation and plotting
1880:"The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis"
661:
Recently there has been some research to identify potential antimicrobial peptides from prokaryotes, aquatic organisms such as fish, and shellfish, and
393:
disordered toroidal-pore model suggests that the AMP is flexible and does not form a stable toroidal structure. The peptide-lipid pore complex becomes
1285:
Papagianni M (September 2003). "Ribosomally synthesized peptides with antimicrobial properties: biosynthesis, structure, function, and applications".
1829:"Large-Scale Analysis of Antimicrobial Activities in Relation to Amphipathicity and Charge Reveals Novel Characterization of Antimicrobial Peptides"
371:
ABOVE: Intact cell membranes in the control group. BELOW: Disrupted cell membranes and leakage of bacterial chromosome (green) in the treated group.
4496:"Towards the improved discovery and design of functional peptides: common features of diverse classes permit generalized prediction of bioactivity"
3017:
Sawaki K, Mizukawa N, Yamaai T, Yoshimoto T, Nakano M, Sugahara T (2002). "High concentration of beta-defensin-2 in oral squamous cell carcinoma".
798:
new small bacterial cell-selective antimicrobial peptides with intracellular mechanisms of action. It has been suggested that direct attachment of
332:
functions that may be involved in the clearance of infection, including the ability to alter host gene expression, act as chemokines and/or induce
1396:
Dhople V, Krukemeyer A, Ramamoorthy A (September 2006). "The human beta-defensin-3, an antibacterial peptide with multiple biological functions".
2073:"A coarse-grained approach to studying the interactions of the antimicrobial peptides aurein 1.2 and maculatin 1.1 with POPG/POPE lipid mixtures"
3234:
Matsuzaki K, Sugishita K, Fujii N, Miyajima K (March 1995). "Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2".
885:
degrading the extracellular peptide and nucleic acid molecules, which if allowed to reach to the bacterial cells may be dangerous for the cells.
124:, and a large proportion (generally >50%) of hydrophobic residues. The secondary structures of these molecules follow 4 themes, including i)
843:
transports D-alanine from the cytoplasm to the surface teichoic acid which reduces the net negative charge by introducing basic amino groups.
5177:
2549:
5001:
598:
2185:
Henzler Wildman KA, Lee DK, Ramamoorthy A (June 2003). "Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37".
3505:"Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides"
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to study and quantify the association to headgroup, insertion into the bilayer, pore formation and eventual disruption of the membrane.
4944:
4174:
3465:
Kulagina NV, Lassman ME, Ligler FS, Taitt CR (October 2005). "Antimicrobial peptides for detection of bacteria in biosensor assays".
1526:
Nguyen LT, Haney EF, Vogel HJ (September 2011). "The expanding scope of antimicrobial peptide structures and their modes of action".
413:
studies have provided an atomic-level resolution explanation of membrane disruption by antimicrobial peptides. In more recent years,
2395:"Differential Interaction of Antimicrobial Peptides with Lipid Structures Studied by Coarse-Grained Molecular Dynamics Simulations"
364:
images (50,000X magnification) displaying the action of an experimental antimicrobial peptide (NN2_0050) on the cell membrane of
905:
lead to resistance, not only to the medical application of the peptides, but to the physiological function of those peptides.
5334:
3985:
3405:
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Hancock RE, Sahl HG (December 2006). "Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies".
1808:
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17:
2128:"MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain"
802:
to the substrate surface decreased nonspecific cell binding and led to improved detection limit for bacterial cells such as
1965:"Antibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistance"
1760:"Real-time quantitative analysis of lipid disordering by aurein 1.2 during membrane adsorption, destabilisation and lysis"
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Research has increased in recent years to develop artificially-engineered mimics of antimicrobial peptides such as
773:
305:
3046:"Surrounding cells affect the gene expression pattern of human beta-defensins in squamous cell carcinoma in vitro"
5319:
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to measure the diffraction patterns of peptide-induced pores within membranes in oriented multilayers or liquids
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to detect loss of intracellular potassium (an indication that bacterial membrane integrity has been compromised)
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4937:
4763:"Prediction of Antitubercular Peptides From Sequence Information Using Ensemble Classifier and Hybrid Features"
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which demonstrate potential as novel therapeutic agents. Antimicrobial peptides have been demonstrated to kill
1045:, in part due to the prohibitive cost of producing naturally-derived AMPs. An example of this is the facially
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3595:"Role of YadA in resistance of Yersinia enterocolitica to phagocytosis by human polymorphonuclear leukocytes"
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Several methods have been used to determine the mechanisms of antimicrobial peptide activity. In particular,
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Turnidge JD, Bell JM (1996). "Susceptibility testing of Antimicrobials in liquid media". In Lorian V (ed.).
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The interaction of antimicrobial peptides with membrane targets can be limited by capsule polysaccharide of
5163:
4910:
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4116:"Structure-function analysis of Avian β-defensin-6 and β-defensin-12: role of charge and disulfide bridges"
3130:"Biosynthesis, structure and biological function of cholesterol glucoside in Helicobacter pylori: A review"
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Bacteria produce proteolytic enzymes, which may degrade antimicrobial peptides leading to their resistance.
361:
3544:
Campos MA, Vargas MA, Regueiro V, Llompart CM, Albertí S, Bengoechea JA (December 2004). Weiser JN (ed.).
1320:
Sitaram N, Nagaraj R (2002). "Host-defense antimicrobial peptides: importance of structure for activity".
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4880:
2662:"The antimicrobial peptide defensin cooperates with tumour necrosis factor to drive tumour cell death in
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to measure the orientation and secondary structure of an antimicrobial peptide bound to a lipid bilayer
723:
4057:"Differential activity of lytic α-helical peptides on lactobacilli and lactobacilli-derived liposomes"
1671:
Brogden KA (March 2005). "Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?".
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4904:
3821:"Bis-(3'-5')-cyclic dimeric GMP regulates antimicrobial peptide resistance in Pseudomonas aeruginosa"
3644:"Sap transporter mediated import and subsequent degradation of antimicrobial peptides in Haemophilus"
4657:"Prediction of Antimicrobial Potential of a Chemically Modified Peptide From Its Tertiary Structure"
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Kalsy M, Tonk M, Hardt M, Dobrindt U, Zdybicka-Barabas A, Cytrynska M, et al. (February 2020).
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Szymanowski F, Balatti GE, Ambroggio E, Hugo AA, Martini MF, Fidelio GD, et al. (June 2019).
2222:"X-ray structure of a carpet-like antimicrobial defensin-phospholipid membrane disruption complex"
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Guilhelmelli F, Vilela N, Albuquerque P, Derengowski L, Silva-Pereira I, Kyaw CM (December 2013).
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In addition, there are also other factors that will affect the selectivity. It's well known that
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Reddy KV, Yedery RD, Aranha C (December 2004). "Antimicrobial peptides: premises and promises".
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Kohn EM, Shirley DJ, Arotsky L, Picciano AM, Ridgway Z, Urban MW, et al. (February 2018).
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Yeaman MR, Yount NY (March 2003). "Mechanisms of antimicrobial peptide action and resistance".
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also modifies its anionic membranes via MprF with L-lysine, increasing the positive net charge.
766:, even though a small portion of the membrane's outer surfaces contain some negatively charged
88:
56:
3306:"Molecular evolution of animal antimicrobial peptides: widespread moderate positive selection"
2717:"The insect antimicrobial peptide cecropin A disrupts uropathogenic Escherichia coli biofilms"
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domain of human platelet factor IV. Currently, the most widely used antimicrobial peptide is
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Prediction of functional peptides, including antimicrobial peptides, in a protein sequence
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Kudrimoti M, Curtis A, Azawi S, Worden F, Katz S, Adkins D, et al. (December 2016).
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In addition to killing bacteria directly they have been demonstrated to have a number of
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Hein KZ, Takahashi H, Tsumori T, Yasui Y, Nanjoh Y, Toga T, et al. (October 2015).
198:, bombinin, brevinin-1, esculentins and buforin II from amphibians, CAP18 from rabbits,
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2499:"New insights on Drosophila antimicrobial peptide function in host defense and beyond"
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Essential Metals in Medicine:Therapeutic Use and Toxicity of Metal Ions in the Clinic
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1609:"Disulphide-reduced psoriasin is a human apoptosis-inducing broad-spectrum fungicide"
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transports AMPs into the interior of the cell, where they are degraded. Furthermore,
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Agrawal P, Bhalla S, Chaudhary K, Kumar R, Sharma M, Raghava GP (26 February 2018).
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Matsuzaki K (August 2009). "Control of cell selectivity of antimicrobial peptides".
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to study the molecular behaviour and search for specific peptide-lipid interactions
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Schematic representation of the AMPs mechanisms of action when disrupting membranes.
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3819:
Chua SL, Tan SY, Rybtke MT, Chen Y, Rice SA, Kjelleberg S, et al. (May 2013).
3793:
3755:
3714:
3706:
3665:
3655:
3614:
3606:
3565:
3557:
3516:
3474:
3439:
3393:
3354:
3317:
3278:
3243:
3197:
3149:
3141:
3094:
2991:
2898:
2854:
2819:
2775:
2738:
2728:
2687:
2677:
2632:
2624:
2572:
2564:
2520:
2510:
2483:
2461:
2453:
2416:
2406:
2365:
2355:
2302:
2292:
2279:
Poon IK, Baxter AA, Lay FT, Mills GD, Adda CG, Payne JA, et al. (April 2014).
2251:
2241:
2220:
Järvå M, Lay FT, Phan TK, Humble C, Poon IK, Bleackley MR, et al. (May 2018).
2194:
2157:
2147:
2084:
2027:
1986:
1976:
1932:
1891:
1850:
1840:
1771:
1724:
1680:
1638:
1628:
1573:
1535:
1493:
1489:
1452:
1405:
1368:
1357:"LL-37, the only human member of the cathelicidin family of antimicrobial peptides"
1329:
1294:
1271:
1251:
1213:
1175:
1061:
approved antimicrobial peptide, it is commonly used as an artificial preservative.
1050:
928:
Antimicrobial peptides are produced by species across the tree of life, including:
428:
4347:
Waghu FH, Gopi L, Barai RS, Ramteke P, Nizami B, Idicula-Thomas S (January 2014).
3397:
3384:. Advances in Experimental Medicine and Biology. Vol. 611. pp. 313–315.
2660:
Parvy JP, Yu Y, Dostalova A, Kondo S, Kurjan A, Bulet P, et al. (July 2019).
1937:
1920:
1539:
433:
membrane, as well as specific peptide interactions with lipids, ions and solvent.
4986:
4975:
4862:
4821:
4520:
4073:
4056:
3660:
3358:
2995:
2823:
2628:
2336:
through phosphatidylinositol 4,5-bisphosphate-mediated membrane permeabilization"
2032:
2015:
1776:
1759:
1409:
1373:
1356:
790:
423:
410:
329:
293:
92:
4898:
4398:"DRAMP 3.0: an enhanced comprehensive data repository of antimicrobial peptides"
3546:"Capsule polysaccharide mediates bacterial resistance to antimicrobial peptides"
3145:
4632:
3180:
Zasloff M (January 2002). "Antimicrobial peptides of multicellular organisms".
2246:
1613:
Proceedings of the National Academy of Sciences of the United States of America
1069:
Several bioinformatic databases exist to catalogue antimicrobial peptides. The
719:
644:
474:
to assess the formation and stability of an antimicrobial-peptide-induced pore
466:
to measure ability of antimicrobial peptides to permeabilize membrane vesicles
418:
345:
313:
133:
5155:
4849:
4214:
4132:
4114:
Yang M, Zhang C, Zhang X, Zhang MZ, Rottinghaus GE, Zhang S (September 2016).
3977:
2902:
2858:
2733:
2568:
2515:
2498:
2411:
2088:
1845:
1728:
1577:
1179:
522:
to measure the proteomic response of microorganisms to antimicrobial peptides
5313:
5143:
5049:
4874:
4833:
4814:
4779:
4728:
4673:
3760:
3743:
2393:
Balatti GE, Ambroggio EE, Fidelio GD, Martini MF, Pickholz M (October 2017).
2096:
2041:
1981:
1758:
Lee TH, Heng C, Swann MJ, Gehman JD, Separovic F, Aguilar MI (October 2010).
1333:
888:
763:
743:
297:
80:
76:
72:
4247:
Shin JM, Gwak JW, Kamarajan P, Fenno JC, Rickard AH, Kapila YL (June 2016).
3521:
3504:
2281:"Phosphoinositide-mediated oligomerization of a defensin induces cell lysis"
2072:
1633:
5207:
5059:
4990:
4798:
4747:
4692:
4641:
4590:
4539:
4480:
4431:
4382:
4333:
4282:
4233:
4151:
4082:
3995:
3954:
3903:
3885:
3854:
3805:
3679:
3579:
3530:
3486:
3451:
3415:
3366:
3331:
3290:
3209:
3163:
3106:
3061:
3030:
3003:
2910:
2866:
2831:
2787:
2752:
2701:
2646:
2586:
2534:
2475:
2430:
2379:
2360:
2316:
2265:
2206:
2171:
2104:
2049:
2016:"Toroidal pores formed by antimicrobial peptides show significant disorder"
2000:
1946:
1905:
1896:
1879:
1864:
1785:
1736:
1692:
1652:
1585:
1547:
1501:
1466:
1417:
1382:
1341:
1306:
1263:
1225:
1187:
1117:
1026:
960:
767:
681:
cells, they themselves also secrete human antimicrobial peptides including
309:
308:. In contrast to many conventional antibiotics these peptides appear to be
4827:
4462:
4413:
4364:
4314:
3769:
3728:
3628:
3255:
3044:
Kida-Takaoka S, Yamaai T, Mizukawa N, Murakami J, Iida S (November 2014).
137:
5298:
5273:
5054:
5039:
5006:
4958:
3836:
1137:
1112:
1001:
936:
794:
751:
698:
694:
affinities towards the bacterial membranes and mammalian cell membranes.
574:
568:
562:
550:
249:
225:
195:
125:
4349:"CAMP: Collection of sequences and structures of antimicrobial peptides"
3642:
Shelton CL, Raffel FK, Beatty WL, Johnson SM, Mason KM (November 2011).
3443:
3247:
2682:
2525:
2297:
1962:
1684:
1563:
1441:"Role of membranes in the activities of antimicrobial cationic peptides"
401:
4581:
4555:"PeptideLocator: prediction of bioactive peptides in protein sequences"
4167:"Synthetic Mimics of Antimicrobial Peptides: A New Wave of Antibiotics"
2550:"Antimicrobial host defence peptides: functions and clinical potential"
2466:
2330:
Järvå M, Phan TK, Lay FT, Caria S, Kvansakul M, Hulett MD (July 2018).
1803:(4th ed.). Baltimore, Md.: Williams and Wilkins. pp. 52–111.
1127:
986:
982:
946:
917:
804:
592:
586:
580:
556:
544:
538:
263:
217:
129:
60:
59:
found among all classes of life. Fundamental differences exist between
4264:
3935:
3797:
3503:
Peschel A, Otto M, Jack RW, Kalbacher H, Jung G, Götz F (March 1999).
3478:
2887:
2198:
1255:
450:
to visualize the effects of antimicrobial peptides on microbial cells
91:, and may also have the ability to enhance immunity by functioning as
5217:
5120:
5077:
1030:
1016:
950:
703:
662:
344:
production, promoting wound healing, and modulating the responses of
333:
245:
165:
121:
64:
4553:
Mooney C, Haslam NJ, Holton TA, Pollastri G, Shields DC (May 2013).
4198:"Role of Cationic Side Chains in the Antimicrobial Activity of C18G"
3870:"Therapeutic antimicrobial peptides may compromise natural immunity"
3201:
3098:
5288:
5283:
5278:
5263:
5247:
5222:
5212:
5044:
4996:
4980:
4298:"A large-scale structural classification of antimicrobial peptides"
997:
978:
970:
799:
682:
601:, bacterial infection against Gram-positive and Gram-negative also.
357:
341:
256:
213:
191:
187:
179:
113:
4855:
4445:
Jhong JH, Chi YH, Li WC, Lin TH, Huang KY, Lee TY (January 2019).
3592:
3043:
2547:
1165:
279:
5115:
4889:
at National Institute for Research in Reproductive Health (NIRRH)
2960:. India: The Printers Mysore. Press Trust of India. 25 April 2019
2927:"In Spiny anteater's milk could be an alternative to antibiotics"
1084:
1079:) is the original and model database for antimicrobial peptides (
974:
810:
758:
outer surfaces of the membranes are usually made of zwitterionic
647:, synergistically clearing infection in vivo (in the insect host
633:
221:
183:
68:
2808:
2548:
Mookherjee N, Anderson MA, Haagsman HP, Davidson DJ (May 2020).
643:(UPEC) cells, either alone or when combined with the antibiotic
4895:- Database of Antimicrobial Activity and Structure of Peptides]
4886:
4494:
Mooney C, Haslam NJ, Pollastri G, Shields DC (8 October 2012).
4054:
3742:
Whitelock JM, Murdoch AD, Iozzo RV, Underwood PA (April 1996).
3233:
1122:
1107:
1046:
1005:
678:
117:
32:
4913:
Bioactive peptide, including antimicrobial peptide, prediction
4604:
Müller AT, Gabernet G, Hiss JA, Schneider G (September 2017).
3741:
2844:
2392:
490:
to measure the different mechanisms of antimicrobial peptides
417:
has been used to delineate in atomic detail how the family of
5293:
3593:
China B, N'Guyen BT, de Bruyere M, Cornelis GR (April 1994).
3016:
2184:
2013:
1815:
National Committee of Laboratory Safety and Standards (NCLSS)
1054:
1042:
1034:
733:
Molecular Basis of Cell Selectivity of Antimicrobial Peptides
210:
rich in proline, arginine, phenylalanine, glycine, tryptophan
4952:
4868:
4493:
3543:
2613:"Studies on anticancer activities of antimicrobial peptides"
2014:
Sengupta D, Leontiadou H, Mark AE, Marrink SJ (2008-10-01).
5230:
5226:
4705:
4603:
4552:
4296:
Lee HT, Lee CC, Yang JR, Lai JZ, Chang KY (February 2015).
3972:. Vol. 19. Berlin: de Gruyter GmbH. pp. 181–202.
2443:
1395:
296:
is a frequent target, but peptides may also interfere with
199:
4836:
Prediction of antimicrobial potential of modified peptides
4195:
3641:
3464:
1918:
605:
2954:"Egg-laying mammal's milk may help for novel antibiotics"
1606:
1354:
822:"AMP resistance" redirects here. Not to be confused with
4396:
Shi GB, Kang XY, Dong FY, Liu YC, Zhu N (January 2022).
3782:
3502:
1355:
Dürr UH, Sudheendra US, Ramamoorthy A (September 2006).
4916:
3967:
1878:
Hunter HN, Fulton DB, Ganz T, Vogel HJ (October 2002).
1080:
397:, with the orientation of the peptide not well defined.
4892:
4246:
2714:
2070:
1559:
1557:
891:
signaling had also been involved in the regulation of
4346:
2659:
2125:
1877:
4101:
Orientations of Proteins in Membranes database (OPM)
4042:
Orientations of Proteins in Membranes database (OPM)
3379:
1958:
1956:
479:
Circular dichroism and orientated circular dichroism
4760:
4113:
1713:
1554:
833:strategies to avoid antimicrobial peptide killing.
620:modifications common to most cancer cells, such as
67:cells that may represent targets for antimicrobial
4761:Usmani SS, Bhalla S, Raghava GP (26 August 2018).
4061:Biochimica et Biophysica Acta (BBA) - Biomembranes
3695:"Multidrug efflux pumps of gram-negative bacteria"
3347:Biochimica et Biophysica Acta (BBA) - Biomembranes
2984:Biochimica et Biophysica Acta (BBA) - Biomembranes
2617:Biochimica et Biophysica Acta (BBA) - Biomembranes
2278:
2219:
2020:Biochimica et Biophysica Acta (BBA) - Biomembranes
1764:Biochimica et Biophysica Acta (BBA) - Biomembranes
1757:
1659:
1479:
1398:Biochimica et Biophysica Acta (BBA) - Biomembranes
1361:Biochimica et Biophysica Acta (BBA) - Biomembranes
742:The cell membranes of bacteria are rich in acidic
27:Class of peptides that have antimicrobial activity
3818:
3229:
3227:
2977:
2975:
2765:
2610:
2578:20.500.11820/1ec38809-e8f2-4684-8bbb-e908ecb5c66e
2329:
2071:Balatti GE, Martini MF, Pickholz M (2018-07-17).
1953:
1203:
426:have now been shown to kill the pathogenic fungi
233:Anionic/cationic peptides forming disulfide bonds
207:Cationic peptide enriched for specific amino acid
5311:
4158:
3867:
3268:
1666:
1664:
1662:
1525:
5185:
4712:Approach for Prediction of Antifungal Peptides"
3498:
3496:
3175:
3173:
3080:
3078:
837:Some microorganisms alter net surface charges.
718:Similarly, it is also believed that increasing
528:
4654:
4395:
3428:
3297:
3224:
2972:
2606:
2604:
2496:
2126:Hallock KJ, Lee DK, Ramamoorthy A (May 2003).
1521:
1519:
1319:
1278:
632:Cecropin A can destroy planktonic and sessile
5171:
4938:
4648:
4444:
4295:
3776:
3458:
3271:International Journal of Antimicrobial Agents
1826:
1792:
1237:
1235:
1206:International Journal of Antimicrobial Agents
283:The modes of action by Antimicrobial peptides
5002:Bactericidal permeability-increasing protein
4815:ADAM (A Database of Anti-Microbial peptides)
4699:
4606:"modlAMP: Python for antimicrobial peptides"
4597:
3686:
3635:
3493:
3170:
3075:
2178:
2119:
1827:Wang CK, Shih LY, Chang KY (November 2017).
1798:
1438:
1199:
1197:
71:. These peptides are potent, broad spectrum
36:Various structures of antimicrobial peptides
4754:
4546:
4487:
4164:
3861:
3537:
3344:
3084:
2601:
1871:
1516:
1432:
1313:
1241:
1159:
5178:
5164:
4945:
4931:
4887:CAMP:Collection of Anti-Microbial Peptides
4883:at Peking University Health Science Center
4438:
4340:
3910:
3586:
2923:
2611:Hoskin DW, Ramamoorthy A (February 2008).
2437:
2213:
1707:
1389:
1284:
1232:
1049:peptide C18G, which was designed from the
4871:Deep Learning based AMP prediction server
4842:at the U.S. National Library of Medicine
4788:
4778:
4737:
4727:
4682:
4672:
4655:Agrawal P, Raghava GP (26 October 2018).
4631:
4621:
4580:
4570:
4529:
4519:
4470:
4421:
4372:
4323:
4313:
4272:
4240:
4223:
4213:
4189:
4141:
4131:
4107:
4072:
3944:
3934:
3893:
3844:
3812:
3759:
3735:
3718:
3669:
3659:
3618:
3569:
3520:
3321:
3303:
3262:
3153:
2981:
2742:
2732:
2691:
2681:
2636:
2576:
2524:
2514:
2465:
2420:
2410:
2369:
2359:
2306:
2296:
2272:
2255:
2245:
2161:
2151:
2031:
1990:
1980:
1936:
1895:
1854:
1844:
1820:
1775:
1642:
1632:
1600:
1473:
1456:
1372:
1194:
627:
611:broad scope of activities AMPs can have.
4865:at University of Nebraska Medical Center
4852:Prediction of anti-tuberculosis peptides
3916:
3422:
3373:
3127:
2934:. Chennai, India: Kasturi & Sons Ltd
2847:Developmental and Comparative Immunology
1751:
1348:
916:
728:
614:
400:
356:
278:
102:
31:
4389:
4289:
4173:. University of Georgia. Archived from
3692:
3338:
3179:
2497:Hanson MA, Lemaitre B (February 2020).
1670:
817:
606:Activity beyond antibacterial functions
352:
14:
5312:
4089:
4030:
3868:Habets MG, Brockhurst MA (June 2012).
726:required for the initial interaction.
5159:
4926:
3825:Antimicrobial Agents and Chemotherapy
3121:
1133:Liver-expressed antimicrobial peptide
1439:Hancock RE, Rozek A (January 2002).
547:, Hepatitis C (oral, cyclic peptide)
4038:"Insect antimicrobial peptides OPM"
3748:The Journal of Biological Chemistry
3509:The Journal of Biological Chemistry
1884:The Journal of Biological Chemistry
389:and cause the death of the microbe.
323:
292:and several filamentous fungi. The
224:from insects, prophenin from pigs,
161:rich in glutamic and aspartic acids
24:
4249:"Biomedical applications of nisin"
4097:"Amphibian antimicrobial peptides"
1801:Antibiotics in Laboratory Medicine
1458:10.1111/j.1574-6968.2002.tb11000.x
966:many from insects and arthropods (
583:, Hepatitis C, oral cyclic peptide
173:Linear cationic α-helical peptides
25:
5351:
4830:Prediction of antifungal peptides
4808:
4165:Niedermaier H (9 February 2012).
3917:Bahar AA, Ren D (November 2013).
3283:10.1016/j.ijantimicag.2008.04.003
3128:Zhang L, Xie J (September 2023).
1218:10.1016/j.ijantimicag.2004.09.005
1064:
656:
132:due to the presence of 2 or more
4877:Anti Tubercular Peptide Database
3711:10.1128/jb.178.20.5853-5859.1996
3562:10.1128/IAI.72.12.7107-7114.2004
3323:10.1111/j.1420-9101.2005.00925.x
2780:10.1111/j.1365-2672.2012.05338.x
2458:10.1016/j.biotechadv.2018.01.004
774:Dual polarisation interferometry
487:Dual polarization interferometry
306:dual polarisation interferometry
5200:Antimicrobial cationic peptides
4840:Antimicrobial+Cationic+Peptides
4359:(Database issue): D1154–D1158.
4253:Journal of Applied Microbiology
4048:
3961:
3611:10.1128/IAI.62.4.1275-1281.1994
3310:Journal of Evolutionary Biology
3037:
3010:
2946:
2917:
2891:Fish & Shellfish Immunology
2881:
2838:
2802:
2768:Journal of Applied Microbiology
2759:
2708:
2653:
2541:
2490:
2386:
2323:
2064:
2007:
1912:
511:Molecular dynamics simulations
4856:Antimicrobial Peptide Database
3304:Tennessen JA (November 2005).
2924:Somasekhar M (24 April 2019).
2557:Nature Reviews. Drug Discovery
1494:10.1016/j.peptides.2006.06.010
1072:Antimicrobial Peptide Database
991:thioester-containing protein 1
668:
13:
1:
5098:Eosinophil-derived neurotoxin
4869:Antimicrobial Peptide Scanner
4623:10.1093/bioinformatics/btx285
4572:10.1093/bioinformatics/btt103
4408:(Database issue): D488–D496.
4302:BioMed Research International
3398:10.1007/978-0-387-73657-0_140
2503:Current Opinion in Immunology
2153:10.1016/S0006-3495(03)70031-9
2077:Journal of Molecular Modeling
1938:10.1016/j.jbiotec.2016.10.010
1540:10.1016/j.tibtech.2011.05.001
1322:Current Pharmaceutical Design
1299:10.1016/S0734-9750(03)00077-6
1153:
565:, HIV, subcutaneous injection
503:Neutron and X-ray diffraction
362:Scanning electron microscopic
274:
5335:Peripheral membrane proteins
4521:10.1371/journal.pone.0045012
4074:10.1016/j.bbamem.2019.03.004
3786:Journal of Proteome Research
3661:10.1371/journal.ppat.1002360
3359:10.1016/j.bbamem.2008.10.005
2996:10.1016/j.bbamem.2008.09.013
2824:10.1016/j.molimm.2015.10.001
2721:npj Biofilms and Microbiomes
2629:10.1016/j.bbamem.2007.11.008
2033:10.1016/j.bbamem.2008.06.007
1777:10.1016/j.bbamem.2010.06.023
1673:Nature Reviews. Microbiology
1410:10.1016/j.bbamem.2006.07.007
1374:10.1016/j.bbamem.2006.03.030
1143:Peripheral membrane proteins
737:
529:Therapeutic research and use
495:Solid-state NMR spectroscopy
455:Atomic emission spectroscopy
164:Maximin H5 from amphibians,
120:or, in acidic environments,
98:
7:
5088:Eosinophil cationic protein
3146:10.1097/MD.0000000000034911
1717:European Biophysics Journal
1101:
1087:, and LAMP (Linking AMPs).
912:
10:
5356:
3693:Nikaido H (October 1996).
2332:"Human β-defensin 2 kills
2247:10.1038/s41467-018-04434-y
821:
783:
724:electrostatic interactions
688:
595:, bacterial infection, IV.
577:, bacterial infections, IV
571:, bacterial infections, IV
559:, bacterial infections, IV
553:, bacterial infections, IV
236:contain 1~3 disulfide bond
5256:
5240:
5198:
5133:
5106:
5068:
5025:
5015:
4965:
4767:Frontiers in Pharmacology
4716:Frontiers in Microbiology
4661:Frontiers in Microbiology
4215:10.3390/molecules23020329
4133:10.1186/s12866-016-0828-y
3978:10.1515/9783110527872-013
2903:10.1016/j.fsi.2014.12.036
2859:10.1016/j.dci.2017.01.019
2734:10.1038/s41522-020-0116-3
2569:10.1038/s41573-019-0058-8
2516:10.1016/j.coi.2019.11.008
2412:10.3390/molecules22101775
2089:10.1007/s00894-018-3747-z
1969:Frontiers in Microbiology
1846:10.3390/molecules22112037
1729:10.1007/s00249-010-0664-1
1578:10.1007/s00284-012-0268-3
1445:FEMS Microbiology Letters
1180:10.1016/j.bcp.2016.09.018
1085:Welcome To Dramp Database
589:, bacterial infection, IV
340:induced pro-inflammatory
4844:Medical Subject Headings
4780:10.3389/fphar.2018.00954
4729:10.3389/fmicb.2018.00323
4674:10.3389/fmicb.2018.02551
3919:"Antimicrobial peptides"
3761:10.1074/jbc.271.17.10079
1982:10.3389/fmicb.2013.00353
1925:Journal of Biotechnology
1334:10.2174/1381612023395358
1168:Biochemical Pharmacology
395:intrinsically disordered
4171:Department of Chemistry
3699:Journal of Bacteriology
3522:10.1074/jbc.274.13.8405
1634:10.1073/pnas.1511197112
1528:Trends in Biotechnology
1244:Pharmacological Reviews
712:transmembrane potential
336:production, inhibiting
5320:Antimicrobial peptides
5140:platelet alpha-granule
4451:Nucleic Acids Research
4402:Nucleic Acids Research
4353:Nucleic Acids Research
3886:10.1098/rsbl.2011.1203
3599:Infection and Immunity
3550:Infection and Immunity
2446:Biotechnology Advances
2361:10.1126/sciadv.aat0979
1897:10.1074/jbc.M205305200
1287:Biotechnology Advances
925:
898:Pseudomonas aeruginosa
734:
628:Antibiofilm properties
541:for pneumonia, topical
406:
372:
284:
108:
89:transmembrane channels
57:innate immune response
41:Antimicrobial peptides
37:
5093:Eosinophil peroxidase
2226:Nature Communications
920:
893:antimicrobial peptide
867:Hemophilus influenzae
852:Klebsiella pneumoniae
840:Staphylococcus aureus
829:Bacteria use various
824:Ampicillin resistance
732:
615:Anticancer properties
471:Ion channel formation
415:X-ray crystallography
404:
385:functioning properly.
360:
282:
252:from horseshoe crabs;
106:
49:host defence peptides
35:
18:Antimicrobial peptide
5035:Alkaline phosphatase
4967:Azurophilic granules
3837:10.1128/AAC.02499-12
3467:Analytical Chemistry
3134:Medicine (Baltimore)
3087:Nature Biotechnology
2812:Molecular Immunology
1566:Current Microbiology
1148:Virtual colony count
1081:https://aps.unmc.edu
818:Bacterial resistance
748:phosphatidylglycerol
353:Mechanisms of action
294:cytoplasmic membrane
214:abaecin and drosocin
85:biological membranes
5187:Pore-forming toxins
5083:Major basic protein
4901:at Fudan University
4633:20.500.11850/206770
4512:2012PLoSO...745012M
4463:10.1093/nar/gky1030
4414:10.1093/nar/gkab651
4365:10.1093/nar/gkt1157
4315:10.1155/2015/475062
3754:(17): 10079–10086.
3438:(43): 13007–13017.
3390:2009peyo.book..313L
3248:10.1021/bi00010a034
3194:2002Natur.415..389Z
3050:Anticancer Research
3019:Anticancer Research
2818:(2 Pt B): 421–433.
2683:10.7554/eLife.45061
2352:2018SciA....4..979J
2298:10.7554/elife.01808
2238:2018NatCo...9.1962J
2144:2003BpJ....84.3052H
2132:Biophysical Journal
1890:(40): 37597–37603.
1685:10.1038/nrmicro1098
1625:2015PNAS..11213039H
1619:(42): 13039–13044.
760:phosphatidylcholine
650:Galleria mellonella
4861:2011-07-20 at the
4820:2015-06-17 at the
4177:on 28 October 2016
3382:Peptides for Youth
3312:(Review article).
3184:(Review article).
3089:(Review article).
2986:(Review article).
1029:, alpha- and beta-
953:, and many others)
939:, and many others)
926:
735:
665:such as echidnas.
622:phosphatidylserine
519:Mass spectrometry
407:
373:
338:lipopolysaccharide
285:
241:1 bond: brevinins;
186:, ceratotoxin and
109:
55:) are part of the
38:
5307:
5306:
5153:
5152:
5129:
5128:
5017:Specific granules
4616:(17): 2753–2755.
4457:(D1): D285–D297.
4265:10.1111/jam.13033
3987:978-3-11-052691-2
3936:10.3390/ph6121543
3929:(12): 1543–1575.
3798:10.1021/pr4009223
3705:(20): 5853–5859.
3556:(12): 7107–7114.
3515:(13): 8405–8410.
3479:10.1021/ac050639r
3473:(19): 6504–6508.
3444:10.1021/bi060487+
3407:978-0-387-73656-3
3242:(10): 3423–3429.
3188:(6870): 389–395.
3093:(12): 1551–1557.
3056:(11): 6443–6449.
2199:10.1021/bi0273563
2193:(21): 6545–6558.
2026:(10): 2308–2317.
1810:978-0-683-05169-8
1770:(10): 1977–1986.
1488:(11): 2614–2623.
1256:10.1124/pr.55.1.2
1057:; being the only
996:amphibia, frogs (
526:
525:
302:protein synthesis
272:
271:
16:(Redirected from
5347:
5269:Diphtheria toxin
5180:
5173:
5166:
5157:
5156:
5023:
5022:
4987:serine proteases
4953:Contents of the
4947:
4940:
4933:
4924:
4923:
4803:
4802:
4792:
4782:
4758:
4752:
4751:
4741:
4731:
4703:
4697:
4696:
4686:
4676:
4652:
4646:
4645:
4635:
4625:
4601:
4595:
4594:
4584:
4574:
4565:(9): 1120–1126.
4550:
4544:
4543:
4533:
4523:
4491:
4485:
4484:
4474:
4442:
4436:
4435:
4425:
4393:
4387:
4386:
4376:
4344:
4338:
4337:
4327:
4317:
4293:
4287:
4286:
4276:
4259:(6): 1449–1465.
4244:
4238:
4237:
4227:
4217:
4193:
4187:
4186:
4184:
4182:
4162:
4156:
4155:
4145:
4135:
4120:BMC Microbiology
4111:
4105:
4104:
4093:
4087:
4086:
4076:
4067:(6): 1069–1077.
4052:
4046:
4045:
4034:
4028:
4027:
4021:
4017:
4015:
4007:
3965:
3959:
3958:
3948:
3938:
3914:
3908:
3907:
3897:
3865:
3859:
3858:
3848:
3831:(5): 2066–2075.
3816:
3810:
3809:
3792:(3): 1345–1358.
3780:
3774:
3773:
3763:
3739:
3733:
3732:
3722:
3690:
3684:
3683:
3673:
3663:
3654:(11): e1002360.
3639:
3633:
3632:
3622:
3605:(4): 1275–1281.
3590:
3584:
3583:
3573:
3541:
3535:
3534:
3524:
3500:
3491:
3490:
3462:
3456:
3455:
3426:
3420:
3419:
3377:
3371:
3370:
3342:
3336:
3335:
3325:
3316:(6): 1387–1394.
3301:
3295:
3294:
3266:
3260:
3259:
3231:
3222:
3221:
3177:
3168:
3167:
3157:
3125:
3119:
3118:
3082:
3073:
3072:
3070:
3068:
3041:
3035:
3034:
3025:(4): 2103–2107.
3014:
3008:
3007:
2990:(8): 1687–1692.
2979:
2970:
2969:
2967:
2965:
2950:
2944:
2943:
2941:
2939:
2929:
2921:
2915:
2914:
2885:
2879:
2878:
2842:
2836:
2835:
2806:
2800:
2799:
2763:
2757:
2756:
2746:
2736:
2712:
2706:
2705:
2695:
2685:
2657:
2651:
2650:
2640:
2608:
2599:
2598:
2580:
2554:
2545:
2539:
2538:
2528:
2518:
2494:
2488:
2487:
2469:
2441:
2435:
2434:
2424:
2414:
2390:
2384:
2383:
2373:
2363:
2340:Science Advances
2334:Candida albicans
2327:
2321:
2320:
2310:
2300:
2276:
2270:
2269:
2259:
2249:
2217:
2211:
2210:
2182:
2176:
2175:
2165:
2155:
2138:(5): 3052–3060.
2123:
2117:
2116:
2068:
2062:
2061:
2035:
2011:
2005:
2004:
1994:
1984:
1960:
1951:
1950:
1940:
1916:
1910:
1909:
1899:
1875:
1869:
1868:
1858:
1848:
1824:
1818:
1817:
1796:
1790:
1789:
1779:
1755:
1749:
1748:
1711:
1705:
1704:
1668:
1657:
1656:
1646:
1636:
1604:
1598:
1597:
1561:
1552:
1551:
1523:
1514:
1513:
1477:
1471:
1470:
1460:
1436:
1430:
1429:
1404:(9): 1499–1512.
1393:
1387:
1386:
1376:
1367:(9): 1408–1425.
1352:
1346:
1345:
1317:
1311:
1310:
1282:
1276:
1275:
1239:
1230:
1229:
1201:
1192:
1191:
1163:
1074:
1073:
463:Fluorescent dyes
436:
435:
429:Candida albicans
330:immunomodulatory
324:Immunomodulation
176:lack in cysteine
158:Anionic peptides
144:
143:
93:immunomodulators
21:
5355:
5354:
5350:
5349:
5348:
5346:
5345:
5344:
5340:Insect immunity
5310:
5309:
5308:
5303:
5257:Other, nonhuman
5252:
5236:
5194:
5184:
5154:
5149:
5125:
5102:
5064:
5011:
4976:Myeloperoxidase
4961:
4951:
4863:Wayback Machine
4822:Wayback Machine
4811:
4806:
4759:
4755:
4704:
4700:
4653:
4649:
4602:
4598:
4551:
4547:
4492:
4488:
4443:
4439:
4394:
4390:
4345:
4341:
4294:
4290:
4245:
4241:
4194:
4190:
4180:
4178:
4163:
4159:
4112:
4108:
4095:
4094:
4090:
4053:
4049:
4036:
4035:
4031:
4019:
4018:
4009:
4008:
3988:
3966:
3962:
3923:Pharmaceuticals
3915:
3911:
3874:Biology Letters
3866:
3862:
3817:
3813:
3781:
3777:
3740:
3736:
3691:
3687:
3640:
3636:
3591:
3587:
3542:
3538:
3501:
3494:
3463:
3459:
3427:
3423:
3408:
3378:
3374:
3343:
3339:
3302:
3298:
3267:
3263:
3232:
3225:
3202:10.1038/415389a
3178:
3171:
3126:
3122:
3099:10.1038/nbt1267
3083:
3076:
3066:
3064:
3042:
3038:
3015:
3011:
2980:
2973:
2963:
2961:
2952:
2951:
2947:
2937:
2935:
2922:
2918:
2886:
2882:
2843:
2839:
2807:
2803:
2764:
2760:
2713:
2709:
2658:
2654:
2609:
2602:
2552:
2546:
2542:
2495:
2491:
2442:
2438:
2391:
2387:
2346:(7): eaat0979.
2328:
2324:
2277:
2273:
2218:
2214:
2183:
2179:
2124:
2120:
2069:
2065:
2012:
2008:
1961:
1954:
1917:
1913:
1876:
1872:
1825:
1821:
1811:
1797:
1793:
1756:
1752:
1712:
1708:
1669:
1660:
1605:
1601:
1562:
1555:
1524:
1517:
1478:
1474:
1437:
1433:
1394:
1390:
1353:
1349:
1318:
1314:
1283:
1279:
1240:
1233:
1202:
1195:
1164:
1160:
1156:
1104:
1071:
1070:
1067:
1035:regIII peptides
915:
827:
820:
786:
740:
691:
677:With regard to
671:
659:
630:
617:
608:
531:
424:beta-defensin 2
419:plant defensins
411:solid-state NMR
355:
346:dendritic cells
326:
277:
134:disulfide bonds
101:
47:), also called
28:
23:
22:
15:
12:
11:
5:
5353:
5343:
5342:
5337:
5332:
5327:
5322:
5305:
5304:
5302:
5301:
5296:
5291:
5286:
5281:
5276:
5271:
5266:
5260:
5258:
5254:
5253:
5251:
5250:
5244:
5242:
5238:
5237:
5235:
5234:
5220:
5215:
5210:
5204:
5202:
5196:
5195:
5183:
5182:
5175:
5168:
5160:
5151:
5150:
5148:
5147:
5134:
5131:
5130:
5127:
5126:
5124:
5123:
5118:
5112:
5110:
5104:
5103:
5101:
5100:
5095:
5090:
5085:
5080:
5074:
5072:
5066:
5065:
5063:
5062:
5057:
5052:
5047:
5042:
5037:
5031:
5029:
5020:
5013:
5012:
5010:
5009:
5004:
4999:
4994:
4983:
4978:
4972:
4970:
4963:
4962:
4950:
4949:
4942:
4935:
4927:
4921:
4920:
4914:
4908:
4905:PeptideLocator
4902:
4896:
4890:
4884:
4878:
4872:
4866:
4853:
4847:
4837:
4831:
4825:
4824:at ntou.edu.tw
4810:
4809:External links
4807:
4805:
4804:
4753:
4698:
4647:
4610:Bioinformatics
4596:
4559:Bioinformatics
4545:
4506:(10): e45012.
4486:
4437:
4388:
4339:
4288:
4239:
4188:
4157:
4106:
4088:
4047:
4029:
4020:|journal=
3986:
3960:
3909:
3880:(3): 416–418.
3860:
3811:
3775:
3734:
3685:
3648:PLOS Pathogens
3634:
3585:
3536:
3492:
3457:
3421:
3406:
3372:
3353:(2): 333–344.
3337:
3296:
3277:(2): 130–138.
3261:
3223:
3169:
3140:(36): e34911.
3120:
3074:
3036:
3009:
2971:
2945:
2916:
2897:(2): 364–374.
2880:
2837:
2801:
2774:(4): 723–736.
2758:
2707:
2652:
2623:(2): 357–375.
2600:
2563:(5): 311–332.
2540:
2489:
2452:(2): 415–429.
2436:
2385:
2322:
2271:
2212:
2177:
2118:
2063:
2006:
1952:
1911:
1870:
1819:
1809:
1791:
1750:
1723:(4): 503–514.
1706:
1679:(3): 238–250.
1658:
1599:
1572:(3): 271–278.
1553:
1534:(9): 464–472.
1515:
1472:
1451:(2): 143–149.
1431:
1388:
1347:
1328:(9): 727–742.
1312:
1293:(6): 465–499.
1277:
1231:
1212:(6): 536–547.
1193:
1174:(6): 117–138.
1157:
1155:
1152:
1151:
1150:
1145:
1140:
1135:
1130:
1125:
1120:
1115:
1110:
1103:
1100:
1066:
1065:Bioinformatics
1063:
1039:
1038:
1020:
1009:
994:
964:
954:
940:
914:
911:
902:
901:
895:resistance in
886:
882:
879:
875:
862:
855:
848:
819:
816:
785:
782:
776:has been used
739:
736:
720:ionic strength
690:
687:
670:
667:
658:
657:Other research
655:
645:nalidixic acid
638:uropathogenic
629:
626:
616:
613:
607:
604:
603:
602:
596:
590:
584:
578:
572:
566:
560:
554:
548:
542:
530:
527:
524:
523:
520:
516:
515:
512:
508:
507:
504:
500:
499:
496:
492:
491:
488:
484:
483:
480:
476:
475:
472:
468:
467:
464:
460:
459:
456:
452:
451:
448:
444:
443:
440:
399:
398:
390:
386:
382:
354:
351:
325:
322:
314:bacteriostatic
276:
273:
270:
269:
268:
267:
266:in fruit flies
260:
253:
242:
237:
234:
230:
229:
211:
208:
204:
203:
190:from insects,
177:
174:
170:
169:
162:
159:
155:
154:
151:
150:characteristic
148:
100:
97:
73:antimicrobials
26:
9:
6:
4:
3:
2:
5352:
5341:
5338:
5336:
5333:
5331:
5330:Immune system
5328:
5326:
5323:
5321:
5318:
5317:
5315:
5300:
5297:
5295:
5292:
5290:
5287:
5285:
5282:
5280:
5277:
5275:
5272:
5270:
5267:
5265:
5262:
5261:
5259:
5255:
5249:
5246:
5245:
5243:
5239:
5232:
5228:
5224:
5221:
5219:
5216:
5214:
5211:
5209:
5206:
5205:
5203:
5201:
5197:
5192:
5188:
5181:
5176:
5174:
5169:
5167:
5162:
5161:
5158:
5146:
5145:
5144:dense granule
5141:
5136:
5135:
5132:
5122:
5119:
5117:
5114:
5113:
5111:
5109:
5105:
5099:
5096:
5094:
5091:
5089:
5086:
5084:
5081:
5079:
5076:
5075:
5073:
5071:
5067:
5061:
5058:
5056:
5053:
5051:
5050:NADPH oxidase
5048:
5046:
5043:
5041:
5038:
5036:
5033:
5032:
5030:
5028:
5024:
5021:
5018:
5014:
5008:
5005:
5003:
5000:
4998:
4995:
4992:
4988:
4984:
4982:
4979:
4977:
4974:
4973:
4971:
4968:
4964:
4960:
4956:
4948:
4943:
4941:
4936:
4934:
4929:
4928:
4925:
4918:
4915:
4912:
4911:PeptideRanker
4909:
4906:
4903:
4900:
4897:
4894:
4891:
4888:
4885:
4882:
4879:
4876:
4873:
4870:
4867:
4864:
4860:
4857:
4854:
4851:
4848:
4845:
4841:
4838:
4835:
4832:
4829:
4826:
4823:
4819:
4816:
4813:
4812:
4800:
4796:
4791:
4786:
4781:
4776:
4772:
4768:
4764:
4757:
4749:
4745:
4740:
4735:
4730:
4725:
4721:
4717:
4713:
4711:
4702:
4694:
4690:
4685:
4680:
4675:
4670:
4666:
4662:
4658:
4651:
4643:
4639:
4634:
4629:
4624:
4619:
4615:
4611:
4607:
4600:
4592:
4588:
4583:
4578:
4573:
4568:
4564:
4560:
4556:
4549:
4541:
4537:
4532:
4527:
4522:
4517:
4513:
4509:
4505:
4501:
4497:
4490:
4482:
4478:
4473:
4468:
4464:
4460:
4456:
4452:
4448:
4441:
4433:
4429:
4424:
4419:
4415:
4411:
4407:
4403:
4399:
4392:
4384:
4380:
4375:
4370:
4366:
4362:
4358:
4354:
4350:
4343:
4335:
4331:
4326:
4321:
4316:
4311:
4307:
4303:
4299:
4292:
4284:
4280:
4275:
4270:
4266:
4262:
4258:
4254:
4250:
4243:
4235:
4231:
4226:
4221:
4216:
4211:
4207:
4203:
4199:
4192:
4176:
4172:
4168:
4161:
4153:
4149:
4144:
4139:
4134:
4129:
4125:
4121:
4117:
4110:
4102:
4098:
4092:
4084:
4080:
4075:
4070:
4066:
4062:
4058:
4051:
4043:
4039:
4033:
4025:
4013:
4005:
4001:
3997:
3993:
3989:
3983:
3979:
3975:
3971:
3964:
3956:
3952:
3947:
3942:
3937:
3932:
3928:
3924:
3920:
3913:
3905:
3901:
3896:
3891:
3887:
3883:
3879:
3875:
3871:
3864:
3856:
3852:
3847:
3842:
3838:
3834:
3830:
3826:
3822:
3815:
3807:
3803:
3799:
3795:
3791:
3787:
3779:
3771:
3767:
3762:
3757:
3753:
3749:
3745:
3738:
3730:
3726:
3721:
3716:
3712:
3708:
3704:
3700:
3696:
3689:
3681:
3677:
3672:
3667:
3662:
3657:
3653:
3649:
3645:
3638:
3630:
3626:
3621:
3616:
3612:
3608:
3604:
3600:
3596:
3589:
3581:
3577:
3572:
3567:
3563:
3559:
3555:
3551:
3547:
3540:
3532:
3528:
3523:
3518:
3514:
3510:
3506:
3499:
3497:
3488:
3484:
3480:
3476:
3472:
3468:
3461:
3453:
3449:
3445:
3441:
3437:
3433:
3425:
3417:
3413:
3409:
3403:
3399:
3395:
3391:
3387:
3383:
3376:
3368:
3364:
3360:
3356:
3352:
3348:
3341:
3333:
3329:
3324:
3319:
3315:
3311:
3307:
3300:
3292:
3288:
3284:
3280:
3276:
3272:
3265:
3257:
3253:
3249:
3245:
3241:
3237:
3230:
3228:
3219:
3215:
3211:
3207:
3203:
3199:
3195:
3191:
3187:
3183:
3176:
3174:
3165:
3161:
3156:
3151:
3147:
3143:
3139:
3135:
3131:
3124:
3116:
3112:
3108:
3104:
3100:
3096:
3092:
3088:
3081:
3079:
3063:
3059:
3055:
3051:
3047:
3040:
3032:
3028:
3024:
3020:
3013:
3005:
3001:
2997:
2993:
2989:
2985:
2978:
2976:
2959:
2958:Deccan Herald
2955:
2949:
2933:
2928:
2920:
2912:
2908:
2904:
2900:
2896:
2892:
2884:
2876:
2872:
2868:
2864:
2860:
2856:
2852:
2848:
2841:
2833:
2829:
2825:
2821:
2817:
2813:
2805:
2797:
2793:
2789:
2785:
2781:
2777:
2773:
2769:
2762:
2754:
2750:
2745:
2740:
2735:
2730:
2726:
2722:
2718:
2711:
2703:
2699:
2694:
2689:
2684:
2679:
2675:
2671:
2667:
2665:
2656:
2648:
2644:
2639:
2634:
2630:
2626:
2622:
2618:
2614:
2607:
2605:
2596:
2592:
2588:
2584:
2579:
2574:
2570:
2566:
2562:
2558:
2551:
2544:
2536:
2532:
2527:
2522:
2517:
2512:
2508:
2504:
2500:
2493:
2485:
2481:
2477:
2473:
2468:
2463:
2459:
2455:
2451:
2447:
2440:
2432:
2428:
2423:
2418:
2413:
2408:
2404:
2400:
2396:
2389:
2381:
2377:
2372:
2367:
2362:
2357:
2353:
2349:
2345:
2341:
2337:
2335:
2326:
2318:
2314:
2309:
2304:
2299:
2294:
2290:
2286:
2282:
2275:
2267:
2263:
2258:
2253:
2248:
2243:
2239:
2235:
2231:
2227:
2223:
2216:
2208:
2204:
2200:
2196:
2192:
2188:
2181:
2173:
2169:
2164:
2159:
2154:
2149:
2145:
2141:
2137:
2133:
2129:
2122:
2114:
2110:
2106:
2102:
2098:
2094:
2090:
2086:
2082:
2078:
2074:
2067:
2059:
2055:
2051:
2047:
2043:
2039:
2034:
2029:
2025:
2021:
2017:
2010:
2002:
1998:
1993:
1988:
1983:
1978:
1974:
1970:
1966:
1959:
1957:
1948:
1944:
1939:
1934:
1930:
1926:
1922:
1915:
1907:
1903:
1898:
1893:
1889:
1885:
1881:
1874:
1866:
1862:
1857:
1852:
1847:
1842:
1838:
1834:
1830:
1823:
1816:
1812:
1806:
1802:
1795:
1787:
1783:
1778:
1773:
1769:
1765:
1761:
1754:
1746:
1742:
1738:
1734:
1730:
1726:
1722:
1718:
1710:
1702:
1698:
1694:
1690:
1686:
1682:
1678:
1674:
1667:
1665:
1663:
1654:
1650:
1645:
1640:
1635:
1630:
1626:
1622:
1618:
1614:
1610:
1603:
1595:
1591:
1587:
1583:
1579:
1575:
1571:
1567:
1560:
1558:
1549:
1545:
1541:
1537:
1533:
1529:
1522:
1520:
1511:
1507:
1503:
1499:
1495:
1491:
1487:
1483:
1476:
1468:
1464:
1459:
1454:
1450:
1446:
1442:
1435:
1427:
1423:
1419:
1415:
1411:
1407:
1403:
1399:
1392:
1384:
1380:
1375:
1370:
1366:
1362:
1358:
1351:
1343:
1339:
1335:
1331:
1327:
1323:
1316:
1308:
1304:
1300:
1296:
1292:
1288:
1281:
1273:
1269:
1265:
1261:
1257:
1253:
1249:
1245:
1238:
1236:
1227:
1223:
1219:
1215:
1211:
1207:
1200:
1198:
1189:
1185:
1181:
1177:
1173:
1169:
1162:
1158:
1149:
1146:
1144:
1141:
1139:
1136:
1134:
1131:
1129:
1126:
1124:
1121:
1119:
1116:
1114:
1111:
1109:
1106:
1105:
1099:
1096:
1092:
1088:
1086:
1082:
1078:
1062:
1060:
1056:
1052:
1048:
1044:
1036:
1032:
1028:
1027:cathelicidins
1025:
1022:and mammals (
1021:
1018:
1014:
1010:
1008:, and others)
1007:
1003:
999:
995:
992:
988:
984:
980:
976:
972:
969:
965:
962:
959:
955:
952:
948:
945:
941:
938:
935:
931:
930:
929:
923:
919:
910:
906:
900:
899:
894:
890:
889:Cyclic-di-GMP
887:
883:
880:
876:
873:
872:H. influenzae
869:
868:
864:Non-typeable
863:
859:
856:
853:
849:
846:
842:
841:
836:
835:
834:
832:
825:
815:
813:
812:
807:
806:
801:
796:
792:
781:
779:
775:
771:
769:
765:
764:sphingomyelin
761:
755:
753:
749:
745:
744:phospholipids
731:
727:
725:
721:
716:
713:
710:Besides, the
708:
706:
705:
700:
695:
686:
684:
680:
675:
666:
664:
654:
652:
651:
646:
642:
641:
635:
625:
623:
612:
600:
597:
594:
591:
588:
585:
582:
579:
576:
573:
570:
567:
564:
561:
558:
555:
552:
549:
546:
543:
540:
537:
536:
535:
521:
518:
517:
513:
510:
509:
505:
502:
501:
497:
494:
493:
489:
486:
485:
481:
478:
477:
473:
470:
469:
465:
462:
461:
457:
454:
453:
449:
446:
445:
442:Applications
441:
438:
437:
434:
431:
430:
425:
420:
416:
412:
403:
396:
391:
387:
383:
379:
378:
377:
370:
368:(K12 MG1655)
367:
363:
359:
350:
347:
343:
339:
335:
331:
321:
317:
315:
311:
307:
303:
299:
295:
291:
281:
265:
262:more than 3:
261:
258:
254:
251:
247:
243:
240:
239:
238:
235:
232:
231:
228:from cattle.
227:
223:
219:
216:, apidaecin,
215:
212:
209:
206:
205:
201:
197:
193:
189:
185:
181:
178:
175:
172:
171:
167:
163:
160:
157:
156:
152:
149:
146:
145:
142:
139:
135:
131:
127:
123:
119:
115:
105:
96:
94:
90:
86:
82:
81:Gram positive
78:
77:Gram negative
74:
70:
66:
62:
58:
54:
50:
46:
42:
34:
30:
19:
5241:Other, human
5208:Cathelicidin
5137:
5060:Cathelicidin
4991:Proteinase 3
4959:granulocytes
4770:
4766:
4756:
4719:
4715:
4709:
4701:
4664:
4660:
4650:
4613:
4609:
4599:
4562:
4558:
4548:
4503:
4499:
4489:
4454:
4450:
4440:
4405:
4401:
4391:
4356:
4352:
4342:
4305:
4301:
4291:
4256:
4252:
4242:
4205:
4201:
4191:
4179:. Retrieved
4175:the original
4170:
4160:
4123:
4119:
4109:
4100:
4091:
4064:
4060:
4050:
4041:
4032:
3969:
3963:
3926:
3922:
3912:
3877:
3873:
3863:
3828:
3824:
3814:
3789:
3785:
3778:
3751:
3747:
3737:
3702:
3698:
3688:
3651:
3647:
3637:
3602:
3598:
3588:
3553:
3549:
3539:
3512:
3508:
3470:
3466:
3460:
3435:
3432:Biochemistry
3431:
3424:
3381:
3375:
3350:
3346:
3340:
3313:
3309:
3299:
3274:
3270:
3264:
3239:
3236:Biochemistry
3235:
3185:
3181:
3137:
3133:
3123:
3090:
3086:
3065:. Retrieved
3053:
3049:
3039:
3022:
3018:
3012:
2987:
2983:
2962:. Retrieved
2957:
2948:
2936:. Retrieved
2932:BusinessLine
2931:
2919:
2894:
2890:
2883:
2850:
2846:
2840:
2815:
2811:
2804:
2771:
2767:
2761:
2724:
2720:
2710:
2673:
2669:
2663:
2655:
2620:
2616:
2560:
2556:
2543:
2526:10871/133705
2506:
2502:
2492:
2449:
2445:
2439:
2405:(10): 1775.
2402:
2398:
2388:
2343:
2339:
2333:
2325:
2288:
2284:
2274:
2229:
2225:
2215:
2190:
2187:Biochemistry
2186:
2180:
2135:
2131:
2121:
2080:
2076:
2066:
2023:
2019:
2009:
1972:
1968:
1928:
1924:
1914:
1887:
1883:
1873:
1839:(11): 2037.
1836:
1832:
1822:
1814:
1800:
1794:
1767:
1763:
1753:
1720:
1716:
1709:
1676:
1672:
1616:
1612:
1602:
1569:
1565:
1531:
1527:
1485:
1481:
1475:
1448:
1444:
1434:
1401:
1397:
1391:
1364:
1360:
1350:
1325:
1321:
1315:
1290:
1286:
1280:
1250:(1): 27–55.
1247:
1243:
1209:
1205:
1171:
1167:
1161:
1138:Paneth cells
1118:Cathelicidin
1097:
1093:
1089:
1076:
1068:
1040:
1023:
1012:
967:
957:
943:
933:
927:
907:
903:
896:
871:
865:
857:
851:
844:
838:
828:
809:
803:
787:
777:
772:
768:gangliosides
756:
741:
717:
709:
702:
696:
692:
676:
672:
660:
648:
639:
631:
618:
609:
532:
427:
408:
374:
365:
327:
318:
310:bactericidal
289:
286:
259:from humans;
250:tachyplesins
202:from humans
182:, andropin,
168:from humans
110:
52:
48:
44:
40:
39:
29:
5299:Pneumolysin
5274:Dermaseptin
5055:Collagenase
5040:Lactoferrin
5007:Collagenase
4582:10197/10121
2467:11336/98840
2232:(1): 1962.
1931:: 115–125.
1113:Bacteriocin
1002:dermaseptin
937:bacteriocin
922:Fruit flies
795:amino acids
752:cardiolipin
699:cholesterol
669:Selectivity
575:Teicoplanin
569:Oritavancin
563:Enfuvirtide
551:Dalbavancin
312:instead of
226:indolicidin
196:dermaseptin
87:, can form
61:prokaryotic
5325:Immunology
5314:Categories
5070:Eosinophil
5027:Neutrophil
4850:AntiTbPred
4308:: 475062.
4208:(2): 329.
4181:27 October
4126:(1): 210.
3067:7 February
2964:17 January
2938:17 January
2664:Drosophila
2291:: e01808.
2083:(8): 208.
1975:(4): 353.
1154:References
1128:Diptericin
1051:C-terminal
987:drosomycin
983:mastoparan
963:, aurelin)
961:hydramacin
956:cnidaria (
947:peptaibols
932:bacteria (
878:resistance
858:Salmonella
831:resistance
805:Salmonella
746:, such as
663:monotremes
624:exposure.
599:Guavanin 2
593:Vancomycin
587:Telavancin
581:Telaprevir
557:Daptomycin
545:Boceprevir
539:Bacitracin
447:Microscopy
275:Activities
264:drosomycin
248:from pig,
218:diptericin
130:β-stranded
65:eukaryotic
5218:Dermcidin
5138:see also
5121:Histamine
5078:Cathepsin
4981:Defensins
4875:AntiTbPdb
4834:AntiMPmod
4710:In Silico
4202:Molecules
4022:ignored (
4012:cite book
3218:205028607
2853:: 37–48.
2595:211526624
2509:: 22–30.
2399:Molecules
2097:0948-5023
2042:0005-2736
1833:Molecules
1031:defensins
1017:defensins
951:plectasin
845:S. aureus
738:Mechanism
704:H. pylori
636:-forming
334:chemokine
257:defensins
255:3 bonds:
246:protegrin
244:2 bonds:
180:Cecropins
166:dermcidin
138:β-hairpin
126:α-helical
122:histidine
99:Structure
5289:Melittin
5284:Magainin
5279:Latarcin
5264:Cecropin
5248:Perforin
5223:Histatin
5213:Defensin
5108:Basophil
5045:Lysozyme
4997:Lysozyme
4985:neutral
4955:granules
4859:Archived
4818:Archived
4799:30210341
4748:29535692
4693:30416494
4667:: 2551.
4642:28472272
4591:23505299
4540:23056189
4500:PLOS ONE
4481:30380085
4432:34390348
4383:24265220
4334:26000295
4283:26678028
4234:29401708
4152:27613063
4083:30878358
4004:73727689
3996:30855108
3955:24287494
3904:22279153
3855:23403434
3806:24437924
3680:22072973
3580:15557634
3531:10085071
3487:16194120
3452:17059217
3416:19400207
3367:19013127
3332:16313451
3291:18586467
3210:11807545
3164:37682174
3155:10489377
3115:22384207
3107:17160061
3062:25368244
3031:12174890
3004:18952049
2911:25575476
2875:22374102
2867:28126555
2832:26477736
2796:19503463
2788:22583565
2753:32051417
2727:(1): 6.
2702:31358113
2647:18078805
2587:32107480
2535:31835066
2476:29330093
2431:29053635
2380:30050988
2317:24692446
2266:29773800
2207:12767238
2172:12719236
2113:51678964
2105:30019106
2058:19387026
2050:18602889
2001:24367355
1947:27746305
1906:12138110
1865:29165350
1786:20599687
1745:22514308
1737:21222117
1701:23625167
1693:15703760
1653:26438863
1594:18671683
1586:23183933
1548:21680034
1510:21104756
1502:16914230
1482:Peptides
1467:11814654
1426:36461159
1418:16978580
1383:16716248
1342:11945168
1307:14499150
1264:12615953
1226:15555874
1188:27663838
1102:See also
1047:cationic
998:magainin
979:melittin
971:cecropin
913:Examples
800:magainin
791:helicity
778:in vitro
683:defensin
381:microbe.
342:cytokine
192:Magainin
188:melittin
114:arginine
69:peptides
5116:Heparin
4917:modlAMP
4790:6121089
4773:: 954.
4739:5834480
4722:: 323.
4684:6212470
4531:3466233
4508:Bibcode
4472:6323920
4423:8728287
4374:3964954
4325:4426897
4274:4866897
4225:6017431
4143:5016922
3946:3873676
3895:3367763
3846:3632963
3770:8626565
3729:8830678
3671:3207918
3629:8132334
3386:Bibcode
3256:7533538
3190:Bibcode
2744:7016129
2693:6667213
2638:2238813
2484:3873934
2422:6151434
2371:6059731
2348:Bibcode
2308:3968744
2257:5958116
2234:Bibcode
2163:1302867
2140:Bibcode
1992:3856679
1856:6150348
1644:4620902
1621:Bibcode
1272:6731487
1011:birds (
975:attacin
942:fungi (
811:E. coli
784:Control
689:Factors
640:E. coli
634:biofilm
439:Methods
366:E. coli
290:E. coli
222:attacin
184:moricin
136:, iii)
4893:DBAASP
4846:(MeSH)
4828:AntiFP
4797:
4787:
4746:
4736:
4691:
4681:
4640:
4589:
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