Previous research showed that C- terminal of human thrombin constitute a novel class of host defense peptides and its proteolytic variants exert antimicrobial effect against both gram- positive and gram - negative bacteria, mediated by membrane disruption as well as immunomodulatory functions, by inhibiting macrophage response to bacterial lipopolysaccharide.The present work is based on some of selected proteolytic variants so called antimicrobial peptides towards biophysical characterization of antimicrobial peptide-membrane interactions including both lipid and non lipid components for example- lipopolysaccharide and lipid A, in order to focus the details of this interplay. Effect of topology and length on peptide interaction with lipopolysaccharide, lipid A and lipid bilayer was investigated for variants of C- terminal of thrombin derived peptides by ellipsometry, circular dichroism and fluorescence spectroscopy. The results show that peptide- membrane binding aspects need to be considered in order to understand the peptide- membrane interaction, resulting antimicrobial effect through membrane rupture as well as anti-inflammatory effect.

Lipopolysaccharide interactions of C-terminal fragments from thrombin

244th National Meeting (2012)

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