Decoupling electrostatic and hydrophobic contributions to the interactions of anti-microbial peptides and model bacterial membranes
We propose a further investigation of the interaction of the antimicrobial peptides AMP2 (designed by NPL to prevent oligomerization) and pexiganan (forms dimers via leucine zipper) with floating DPPC/DPPG bilayers as models for bacterial membranes. Our previous investigation, identified different patterns of adsorption behavior depending on the bilayer fluidity and the availability of hydrophobic residues. From this we were able to make inferences regarding the likely dominant contribution (hydrophobically or electrostatically mediated) to the interaction of the peptide with the membrane. Here we propose to selectively deuterate the charged and uncharged lipid components, and make use of the expected differences in the interference effects that would result from the different structures that might be expected for different binding modes to unequivocally identify these modes. This will be of great benefit to the design of future antimicrobials targetted at attacking the societal challenge of acquired antibiotic resistance in bacteria.
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BARKER Robert and TITMUSS Simon. (2013). Decoupling electrostatic and hydrophobic contributions to the interactions of anti-microbial peptides and model bacterial membranes. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-02-682
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