Biophysical studies of membrane-peptide interactions and silk proteins

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One of the objectives of our research program is to understand the relationship between the structure, dynamics and interactions of the components of the biological membranes and their function. These systems are investigated in our laboratory by a combination of novel solid-state NMR approaches. Complementary results are also obtained by solution NMR, infrared and fluorescence spectroscopy. The dramatic increase in the appearance of multi-drug resistant bacteria has led to considerable efforts to find new ways to fight pathogen resistance. We describe in this proposal the study of the membrane interactions of novel amphipathic cationic peptides that possess the properties of natural antimicrobial peptides. Several aspects will be investigated, such as the orientation and structure of the peptides in membranes and the mechanism of pore formation. The abnormal aggregation of amyloid proteins is found in a variety of diseases. We are interested in the study of the membrane interactions and structure of the peptide TTR (10-20) derived from transthyretin, a 127 amino acid amyloid protein, and of a peptide corresponding to a conserved hydrophobic region in the human prion protein.