The expanding scope of antimicrobial peptide structures and their modes of action
Antimicrobial peptides (AMPs) are an integral part of the innate immune system that protect a host from invading pathogenic bacteria. To help overcome the problem of antimicrobial resistance, cationic AMPs are currently being considered as potential alternatives for antibiotics. Although extremely v...
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Published in | Trends in biotechnology (Regular ed.) Vol. 29; no. 9; pp. 464 - 472 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Cambridge, MA
Elsevier Ltd
01.09.2011
Cell Press Elsevier Limited |
Subjects | |
Online Access | Get full text |
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Summary: | Antimicrobial peptides (AMPs) are an integral part of the innate immune system that protect a host from invading pathogenic bacteria. To help overcome the problem of antimicrobial resistance, cationic AMPs are currently being considered as potential alternatives for antibiotics. Although extremely variable in length, amino acid composition and secondary structure, all peptides can adopt a distinct membrane-bound amphipathic conformation. Recent studies demonstrate that they achieve their antimicrobial activity by disrupting various key cellular processes. Some peptides can even use multiple mechanisms. Moreover, several intact proteins or protein fragments are now being shown to have inherent antimicrobial activity. A better understanding of the structure–activity relationships of AMPs is required to facilitate the rational design of novel antimicrobial agents. |
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Bibliography: | http://dx.doi.org/10.1016/j.tibtech.2011.05.001 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-3 ObjectType-Review-1 |
ISSN: | 0167-7799 1879-3096 |
DOI: | 10.1016/j.tibtech.2011.05.001 |