Structure-activity relationships of an antimicrobial peptide plantaricin s from two-peptide class IIb bacteriocins.

Abstract:

:Class IIb bacteriocins are ribosomally synthesized antimicrobial peptides comprising two different peptides synergistically acting in equal amounts for optimal potency. In this study, we demonstrate for the first time potent (nanomolar) antimicrobial activity of a representative class IIb bacteriocin, plantaricin S (Pls), against four pathogenic gram-positive bacteria, including Listeria monocytogenes. The structure-activity relationships for Pls were studied using activity assays, circular dichroism (CD), and molecular dynamics (MD) simulations. The two Pls peptides and five Pls derived fragments were synthesized. The CD spectra of the Pls and selected fragments revealed helical conformations in aqueous 2,2,2-trifluoroethanol. The MD simulations showed that when the two Pls peptides are in antiparallel orientation, the helical regions interact and align, mediated by strong attraction between conserved GxxxG/AxxxA motifs. The results strongly correlate with the antimicrobial activity suggesting that helix-helix alignment of the two Pls peptides and interaction between the conserved motifs are crucial for interaction with the target cell membrane.

journal_name

J Med Chem

authors

Soliman W,Wang L,Bhattacharjee S,Kaur K

doi

10.1021/jm101540e

subject

Has Abstract

pub_date

2011-04-14 00:00:00

pages

2399-408

issue

7

eissn

0022-2623

issn

1520-4804

journal_volume

54

pub_type

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