Peptide foldamers - structure and function under the influence of high pressure

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Peptide foldamers (3-15 amino acid residues) will be studied aiming at a detailed under-standing of their preferred conformations, which are envisioned to be "frozen out" by applying pressure. Helical alpha,beta- and alpha,alpha,beta,beta-peptides as model compounds and related peptides that show selective binding to Neuropeptide Y (NPY) receptors will be investigated at different pressures in protic solvents (water, buffer, methanol). Moreover, peptide foldamers that are relevant as organocatalysts will be studied, which could benefit from pressure not only by stabilizing catalytically active conformations, but also from the increased dissociation of water, offering higher concentrations of acid and base catalytic sites that has been recognized to be essential for many organocatalytic processes (Dual Catalysis). Thus, more active and selective organocatalysts in organic transformations are envisioned to be developed, moreover, these studies should also allow a better understanding on the function of enzymes under pressure.