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Characterization of the 3_10-Helix in odel Peptides by HRMAS NMR Spectroscopy

机译:HRMAS NMR光谱表征odel肽中的3_10-螺旋

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摘要

A tetra- and a hepta-homo-peptide from the C~alpha-tetrasubstituted Aib (alpha-aminoisobutyric acid) residue were covalently linked to the POEPOP resi by the fragemnt-condensation approach. The conformational preferences of hte two model peptides were determined for the first time on a solid support by means of high-resolution magic angle spinning NMR spectroscopy. The results obtained indicate that the Aib homopeptides adopt a regular 3_10-helical structure even when they are covalently bound to a polymeric matrix, and thus confirm the remarkable conformational stability of the peptides rich in this amino acid. An ATR-FTIR spectroscopic investigation, performed in parallel, also confirmed that these polymer-bound peptides do indeed adopt a helical conformation. The results of this study open the possibility to exploit the peptide-resin conjugates based on C~alpha-tetrasubstituted alpha-amino acids as helpful, structurally organized temperates in molecular recognition studies or as catalysts in asymmetric synthesis.
机译:通过C-α-四取代的Aib(α-氨基异丁酸)残基的四-和七-同肽通过断裂缩合法共价连接到POEPOP残基。通过高分辨率魔角旋转NMR光谱首次确定了两种模型肽在固体支持物上的构象偏好。获得的结果表明,即使Aib同型肽共价结合至聚合物基质,它们仍具有规则的3_10-螺旋结构,因此证实了富含该氨基酸的肽的显着的构象稳定性。并行进行的ATR-FTIR光谱研究还证实,这些聚合物结合的肽确实确实具有螺旋构象。这项研究的结果为开发基于C〜α-四取代的α-氨基酸的肽-树脂结合物成为可能,在分子识别研究中作为有用的,结构化的温带化合物或作为不对称合成的催化剂提供了可能性。

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