Interaction of antimicrobial peptides with biological and model membranes: Structural and charge requirements for activity

257Citations
Citations of this article
209Readers
Mendeley users who have this article in their library.

Abstract

Species right across the evolutionary scale from insects to mammals use peptides as part of their host-defense system to counter microbial infection. The primary structures of a large number of these host-defense peptides have been determined. While there is no primary structure homology, the peptides are characterized by a preponderance of cationic and hydrophobic amino acids. The secondary structures of many of the host-defense peptides have been determined by a variety of techniques. The acyclic peptides tend to adopt helical conformation, especially in media of low dielectric constant, whereas peptides with more than one disulfide bridge adopt β-structures. Detailed investigations have indicated that a majority of these host-defense peptides exert their action by permeabilizing microbial membranes. In this review, we discuss structural and charge requirements for the interaction of endogenous antimicrobial peptides and short peptides that have been derived from them, with membranes.

Cite

CITATION STYLE

APA

Sitaram, N., & Nagaraj, R. (1999, December 15). Interaction of antimicrobial peptides with biological and model membranes: Structural and charge requirements for activity. Biochimica et Biophysica Acta - Biomembranes. https://doi.org/10.1016/S0005-2736(99)00199-6

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free