Abstract
Antimicrobial peptides are important components of innate immunity in species across the evolutionary scale. Unlike therapeutically used antibiotics, this class of peptides exert their activity by permeabilizing bacterial membranes. Despite the seemingly common mechanism of action, there is considerable variation in their primary structures, length and number of positive charges. Host-defense antimicrobial peptides have been the subject of extensive biophysical studies with a view at delineate structural requirements for activity. In this article, the structures of host defence antibacterial peptides and the structural requirements for activity are reviewed.
Keywords: Antimicrobial peptides, amphiphilic alpha-helical peptides, magainins magainin, buforin, seminalplasmin spln, melittin, indolicidin, tritrpticin, defensins
Current Pharmaceutical Design
Title: Host-defense Antimicrobial Peptides: Importance of Structure for Activity
Volume: 8 Issue: 9
Author(s): Narasimhaiah Sitaram and Ramakrishnan Nagaraj
Affiliation:
Keywords: Antimicrobial peptides, amphiphilic alpha-helical peptides, magainins magainin, buforin, seminalplasmin spln, melittin, indolicidin, tritrpticin, defensins
Abstract: Antimicrobial peptides are important components of innate immunity in species across the evolutionary scale. Unlike therapeutically used antibiotics, this class of peptides exert their activity by permeabilizing bacterial membranes. Despite the seemingly common mechanism of action, there is considerable variation in their primary structures, length and number of positive charges. Host-defense antimicrobial peptides have been the subject of extensive biophysical studies with a view at delineate structural requirements for activity. In this article, the structures of host defence antibacterial peptides and the structural requirements for activity are reviewed.
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Cite this article as:
Sitaram Narasimhaiah and Nagaraj Ramakrishnan, Host-defense Antimicrobial Peptides: Importance of Structure for Activity, Current Pharmaceutical Design 2002; 8 (9) . https://dx.doi.org/10.2174/1381612023395358
DOI https://dx.doi.org/10.2174/1381612023395358 |
Print ISSN 1381-6128 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4286 |
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