The Mechanism of Membrane Disruption by Antimicrobial Peptides

Grant number: DP110101866 | Funding period: 2011 - 2013

Completed

Abstract

Bacterial resistance to antibiotics is a growing crisis in modern medicine. Antibacterial peptides from Australian frogs represent a new class of potent and selective antibacterial agents. Understanding how these peptides kill bacteria but not vertebrate cells could lead to the design of new drugs for pharmaceutical and/or clinical purposes.

Related publications (3)

Effect of phosphatidylcholine bilayer thickness and molecular order on the binding of the antimicrobial peptide maculatin 1.1

TH Lee, MA Sani, S Overall, F Separovic, MI Aguilar

2018-02-01

Antimicrobial peptides (AMPs) interact directly with bacterial membrane lipids. Thus, changes in the lipid composition of bacteria..

Proline-15 creates an amphipathic wedge in maculatin 1.1 peptides that drives lipid membrane disruption

MA Sani, TH Lee, MI Aguilar, F Separovic

2015-01-01

The membrane interaction of peptides derived from maculatin 1.1 and caerin 1.1, with the sequence motif of N and C termini of macu..

Membrane interactions and biological activity of antimicrobial peptides from Australian scorpion

K Luna-Ramírez, MA Sani, J Silva-Sanchez, JM Jiménez-Vargas, F Reyna-Flores, KD Winkel, CE Wright, LD Possani, F Separovic

2014-01-01

UyCT peptides are antimicrobial peptides isolated from the venom of the Australian scorpion. The activity of the UyCT peptides aga..

University of Melbourne Researchers

Frances Separovic