Structure-function relationship studies on the frog skin antimicrobial peptide tigerinin 1: design of analogs with improved activity and their action on clinical bacterial isolates.

Abstract:

:Structure-function relationships in antimicrobial peptides have been extensively investigated in order to obtain improved analogs. Most of these studies have targeted either alpha-helical peptides or beta-sheet peptides with multiple disulfide bridges. Tigerinins are short, nonhelical antimicrobial peptides with a single disulfide bridge. In this study, we have synthesized several analogs of tigerinin 1 with an aim to understand the structural basis of activity as well as improve its activity. The studies demonstrate that the loop structure of tigerinin 1 is essential for its optimal activity. However, linearization with increased cationic charges can compensate for loss of loop structure to some extent. Morphology of the cells after treatment with the active analogs shows extensive leakage of cytoplasmic contents. Tigerinin 1 and two of its analogs exhibit impressive activity against a variety of clinical bacterial isolates.

authors

Sitaram N,Sai KP,Singh S,Sankaran K,Nagaraj R

doi

10.1128/aac.46.7.2279-2283.2002

subject

Has Abstract

pub_date

2002-07-01 00:00:00

pages

2279-83

issue

7

eissn

0066-4804

issn

1098-6596

journal_volume

46

pub_type

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