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

肽折叠体（3-15个氨基酸残基）将被研究，旨在详细了解它们的优选构象，设想通过施加压力将其“冻出”。螺旋α，β-和α，α，β，β-肽作为模型化合物和相关肽，显示选择性结合神经肽Y（NPY）受体将在不同的压力下在质子溶剂（水，缓冲液，甲醇）进行研究。此外，将研究与有机催化剂相关的肽折叠体，其不仅可以通过稳定催化活性构象而受益于压力，还可以通过增加水的解离而受益于压力，从而提供更高浓度的酸和碱催化位点，这已被认为是许多有机催化过程（双重催化）所必需的。因此，在有机转化反应中，更活跃和选择性的有机催化剂被设想开发，此外，这些研究也应该允许更好地了解在压力下的酶的功能。

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.