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Antimicrobial peptides

About: Antimicrobial peptides is a research topic. Over the lifetime, 10645 publications have been published within this topic receiving 507688 citations. The topic is also known as: host defense peptide & antimicrobial protein.


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Journal ArticleDOI
TL;DR: The hypothesis that pleurocidin participates in innate mucosal immunity, and it may prove to be a beneficial therapeutic agent, is supported.
Abstract: Antimicrobial peptides are proposed to act as the first line of mucosal host defense by exerting broad-spectrum microbicidal activity against pathogenic microbes. Pleurocidin, a new 25-residue linear antimicrobial peptide, was recently isolated from the skin secretions of winter flounder (Pleuronectes americanus). The present study identifies the cDNA and gene encoding pleurocidin. The pleurocidin gene comprises four exons. Its upstream region demonstrates consensus binding sequences for transcription factors found in host defense genes in mammals, including sequences identical to the NF-IL6 and alpha and gamma interferon response elements. Pleurocidin is predicted to exist as a 68-residue prepropeptide that undergoes proteolytic cleavage of its amino-terminal signal and carboxy-terminal anionic propiece to form the active, mature peptide. Transmission electron microscopy localized pleurocidin to the mucin granules of skin and intestinal goblet cells. Significant synergy was shown to occur between pleurocidin and D-cycloserine targeting Mycobacterium smegmatis. Pleurocidin was functionally active at physiologic concentrations of magnesium and calcium; however, high concentrations of these divalent cations ablated pleurocidin's activity against a standard test strain, Escherichia coli D31. Pleurocidin was tested against bacterial and fungal clinical isolates and showed broad-spectrum antimicrobial activity. Together, these data support the hypothesis that pleurocidin participates in innate mucosal immunity, and it may prove to be a beneficial therapeutic agent.

150 citations

Journal ArticleDOI
TL;DR: In hagfish cathelicidins, the unusual amino acid bromotryptophan may make the active peptides less susceptible to proteolysis for steric reasons, and such protease resistance could extend the pharmacokinetic lifetimes of cathe Licidins in vivo, sustaining antimicrobial activity.

149 citations

Journal ArticleDOI
TL;DR: This brief review aims at providing some illustrative examples on the interaction between amphiphilic peptides and phospholipid membranes an area of significant current interest focusing on antimicrobial peptides.
Abstract: This brief review aims at providing some illustrative examples on the interaction between amphiphilic peptides and phospholipid membranes an area of significant current interest Focusing on antimicrobial peptides factors affecting peptide-membrane interactions are addressed including effects of peptide length charge hydrophobicity secondary structure and topology Effects of membrane composition are also illustrated including effects of membrane charge nature of the polar headgroup and presence of cholesterol and other sterols Throughout novel insights on the importance of peptide adsorption density on membrane stability are emphasized as is the correlation between peptide adsorption peptide induced leakage in model liposome systems peptide-induced lysis of bacteria and bacteria killing (C) 2010 Elsevier Ltd All rights reserved (Less)

149 citations

Journal ArticleDOI
01 Dec 2007-Peptides
TL;DR: The peptide H-KKLFKKILKYL-NH(2) (BP100) showed efficacies in flowers of 63-76% at 100 microM, being more potent than BP76 and only less effective than streptomycin, currently used for fire blight control.

149 citations

Journal ArticleDOI
TL;DR: A potential application of WLBU2 in the treatment of bacterial sepsis is established because of its ability to specifically eliminate P. aeruginosa in coculture with human monocytes or skin fibroblasts without detectable adverse effects to the host cells.
Abstract: Cationic amphipathic peptides have been extensively investigated as a potential source of new antimicrobials that can complement current antibiotic regimens in the face of emerging drug-resistant bacteria. However, the suppression of antimicrobial activity under certain biologically relevant conditions (e.g., serum and physiological salt concentrations) has hampered efforts to develop safe and effective antimicrobial peptides for clinical use. We have analyzed the activity and selectivity of the human peptide LL37 and the de novo engineered antimicrobial peptide WLBU2 in several biologically relevant conditions. The host-derived synthetic peptide LL37 displayed high activity against Pseudomonas aeruginosa but demonstrated staphylococcus-specific sensitivity to NaCl concentrations varying from 50 to 300 mM. Moreover, LL37 potency was variably suppressed in the presence of 1 to 6 mM Mg(2+) and Ca(2+) ions. In contrast, WLBU2 maintained its activity in NaCl and physiologic serum concentrations of Mg(2+) and Ca(2+). WLBU2 is able to kill P. aeruginosa (10(6) CFU/ml) in human serum, with a minimum bactericidal concentration of <9 microM. Conversely, LL37 is inactive in the presence of human serum. Bacterial killing kinetic assays in serum revealed that WLBU2 achieved complete bacterial killing in 20 min. Consistent with these results was the ability of WLBU2 (15 to 20 microM) to eradicate bacteria from ex vivo samples of whole blood. The selectivity of WLBU2 was further demonstrated by its ability to specifically eliminate P. aeruginosa in coculture with human monocytes or skin fibroblasts without detectable adverse effects to the host cells. Finally, WLBU2 displayed potent efficacy against P. aeruginosa in an intraperitoneal infection model using female Swiss Webster mice. These results establish a potential application of WLBU2 in the treatment of bacterial sepsis.

149 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023512
20221,025
2021809
2020844
2019728
2018634