环状沉积肽中酯键构象作用的研究。用能量计算和核磁共振光谱法研究环(- l - ala - l - hmb -)2。

T Kato, H Mizuno, S Lee, H Aoyagi, H Kodama, N Go, T Kato
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引用次数: 0

摘要

通过设计和合成四沉积肽环(- l - ala - l - hmb -)2模型,并对其构象进行理论和实验分析,研究了酯键对肽分子构象的影响。理论分析表明,在全局最小值3 kcal/mol范围内,计算得到的低能构象中的酯键和肽键均为反式扭曲构象。酯键的畸变比肽键大。此外,四个羰基从环主链平面的一侧突出,而侧链从另一侧突出。这些结果与核磁共振测量的实验结果一致;首先,从DMSO-d6的1H-NMR组分推导出的耦合常数与计算出的低能构象的二面角一致;其次,NOE测量结果可以再现计算出的羰基和侧链的构型。从理论和实验结果的一致性来看,该模型四沉积肽在溶液中呈全反式主链构象,该主链构象由于酯键的大畸变而稳定,补偿了仅由l-残基组成的12元环状主链结构所造成的应变。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Survey of conformational role of ester bonds in a cyclic depsipeptide. Study on cyclo(-L-Ala-L-Hmb-)2 by energy calculation and NMR spectroscopy.

The effect of ester bond on the conformation of peptide molecule was studied by designing and synthesizing a model tetradepsipeptide cyclo(-L-Ala-L-Hmb-)2 and by analyzing the conformation both theoretically and experimentally. Theoretical analysis showed that both ester and peptide bonds in the calculated low-energy conformations within 3 kcal/mol of the global minimum take a trans but distorted configuration. The distortion is larger in ester bonds than in peptide bonds. Further, the four carbonyls project from one side of the plane of the cyclic backbone, whereas the side chains project from the other side. These results are consistent with the experimental results obtained by NMR measurement; first, the coupling constant deduced from 1H-NMR species in DMSO-d6 is consistent with the dihedral angles of the calculated low-energy conformations; second, results of NOE measurement can reproduce the calculated configuration of the carbonyls and side chains. From the consistency between theoretical and experimental results, it is concluded that this model tetradepsipeptide takes an all-trans backbone conformation in solution and this backbone conformation is stabilized by large distortion in the ester bond, which compensates the strain resulted from the 12-membered cyclic backbone structure consisting only of L-residues.

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