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Characterization of the 3(10)-helix in model peptides by HRMAS NMR spectroscopy

机译：通过HRMAS NMR光谱表征模型肽中的3（10）-螺旋

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摘要

A tetra- and a hepta-homopeptide from the C-alpha-tetrasubstituted Aib (alpha-aminoisobutyric acid) residue were covalently linked to the POEPOP resin by the fragment-condensation approach. The conformational preferences of the 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 a-amino acids as helpful, structurally organized templates in molecular recognition studies or as catalysts in asymmetric synthesis. [References: 78]
机译：通过片段缩合方法，将来自C-α-四取代的Aib（α-氨基异丁酸）残基的四-和七-同肽共价连接至POEPOP树脂。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同型肽共价结合到聚合物基质上，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具有显着的构象稳定性。并行进行的ATR-FTIR光谱研究还证实，这些与聚合物结合的肽确实确实具有螺旋构象。这项研究的结果为利用基于C-α-四取代的a-氨基酸的肽-树脂结合物作为分子识别研究中有用的，结构化的模板或作为不对称合成的催化剂提供了可能性。 [参考：78]

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