Infrared absorption study of human proinsulin C-peptide fragments in dichloromethane.
Infrared absorption study of human proinsulin C-peptide fragments in dichloromethane.
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DOI：
10.1246/bcsj.59.2445
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发表时间：
1986-08
影响因子：
4
通讯作者：
M. Narita;T. Ogura;Kazuhiro Sato;S. Honda
中科院分区：
文献类型：
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作者：
M. Narita;T. Ogura;Kazuhiro Sato;S. Honda
结合具有极性侧链的肽中间体的构象与溶解度之间的关系，在二氯甲烷中进行人胰岛素原C肽片段的IR光谱构象分析。肽片段中涉及的极性氨基酸残基是Glu（OBzl）、Asp（OBzl）、Gln和Ser（Bzl）。特别地，在较宽的浓度范围内探索了N-H伸缩吸收光谱。基于N-H伸缩带的浓度依赖性，已经表明在3330 cm−1附近的特征N-H伸缩带是由于分子内氢键。分子间氢键也发生在这些肽在很小程度上，引起轻微的浓度依赖性的N-H伸缩带。在Glu（OBzl）和Asp（OBzl）残基的极性侧链被保护的寡肽的构象行为与相应的同源寡肽（Leu）的构象行为相同，表明被保护的极性侧链是一种构象稳定的寡肽。
In connection with the relationship between the conformation and solubility of peptide intermediates having polar side chains, IR spectroscopic conformational analysis of human proinsulin C-peptide fragments was performed in dichloromethane. The polar amino acid residues involved in the peptide fragments are Glu(OBzl), Asp(OBzl), Gin, and Ser(Bzl). Especially, the N–H stretching absorption spectra have been explored over a wide range of concentration. Based on the concentration dependence of the N–H stretching bands, it has been shown that the characteristic N–H stretching band around 3330 cm−1 is due to the intramolecular hydrogen bond. Intermolecular hydrogen bonding also occurs to a small extent in these peptides, giving rise to a slight concentration dependence of the N–H stretching bands. Conformational behaviors of oligopeptides having protected polar side chains of the Glu(OBzl) and Asp(OBzl) residues are just the same as those of the corresponding homooligo(Leu)s, indicating that the protected pol...