Solid-State NMR Investigation of the Membrane-Disrupting Mechanism of Antimicrobial Peptides MSI-78 and MSI-594 Derived from Magainin 2 and Melittin

From: Biophysical Journal | Date: July 1, 2006| Author: Lee, Dong-Kuk; Maloy, Lee; Tan, Anmin; Thennarasu, Sathiah; Ramamoorthy, Ayyalusamy | Copyright information

ABSTRACT

The mechanism of membrane interaction of two amphipathic antimicrobial peptides, MSI-78 and MSI-594, derived from magainin-2 and melittin, is presented. Both the peptides show excellent antimicrobial activity. The 8-anilinonaphthalene-1-sulfonic acid uptake experiment using Escherichia coli cells suggests that the outer membrane permeabilization is mainly due to electrostatic interactions. The interaction of MSI-78 and MSI-594 with lipid membranes was studied using ^sup 31^P a...

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