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.

将研究肽折叠体（3-15 个氨基酸残基），旨在详细了解其首选构象，预计通过施加压力“冻结”这些构象。将在不同压力下在质子溶剂（水、缓冲液、甲醇）中研究作为模型化合物的螺旋 α,β- 和 α,α,β,β-肽以及显示与神经肽 Y (NPY) 受体选择性结合的相关肽。此外，还将研究与有机催化剂相关的肽折叠体，它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，从而提供更高浓度的酸和碱催化位点，这已被认为对许多有机催化过程（双催化）至关重要。因此，预计将开发出在有机转化中更具活性和选择性的有机催化剂，此外，这些研究还应该能够更好地了解酶在压力下的功能。