Abstract
Latarcins are linear antimicrobial peptides purified from the venom of the Lachesana tarabaevi spider. They are highly active against Gram-positive and Gram-negative bacteria with minimum inhibitory concentrations (MIC) at the micromolar level and low hemolytic activity (1, 2). In the present work, a 26 residue peptide Latarcin 2a that adopts a helix-hinge-helix conformation in a membrane mimetic environment (1, 2) was studied as well as a derivative obtained by replacing the Guanine 11 by with Alanine. The interaction of the peptides with phospholipid mono and bilayers were investigated using Langmuir-Blodgett monolayer technique, Atomic Force Microscopy (AFM), calcein leakage assay and UV resonance Raman spectroscopy. Effect of small changes in the primary structure of the peptide on the membrane rupturing activity is discussed.
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