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

肽折叠体——高压影响下的结构和功能

• 批准号: 243147505
• 负责人: Professor Dr. Oliver Reiser
• 金额: --
• 依托单位: Institut für Organische Chemie
• 依托单位国家: 德国
• 项目类别: Research Units
• 财政年份: 2013
• 资助国家: 德国
• 起止时间: 2012-12-31 至 2019-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/243147505?language=en
• 关键词: Peptide; foldamers; structure; function; under

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.

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首选构象，这些构象被设想为通过施加压力“冻结”。螺旋α、β -和α、α、β、β肽作为模型化合物和与神经肽Y （NPY）受体选择性结合的相关肽，将在不同压力的质子溶剂（水、缓冲液、甲醇）中进行研究。此外，将研究与有机催化剂相关的肽折叠物，它不仅可以通过稳定催化活性构象，还可以通过增加水的解离，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所必需的（双催化）。因此，在有机转化中，更多的活性和选择性的有机催化剂将被开发出来，而且这些研究也将使人们更好地了解酶在压力下的功能。