Effect of the environment and role of the pi-pi stacking interactions in the stabilization of the 3(10)-helix conformation in dehydroalanine oligopeptides.

C Alemän
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Abstract

A quantum-mechanical study of the chain-length dependent stability of the extended, 2(7)-ribbon and 3(10)-helix conformations in dehydroalanine (delta Ala) oligopeptides has been performed. To address the study, the oligopeptides delta Ala(n), where n varies from 1 to 6, were computed by using the semiempirical AMI methodology. Cooperative free-energy effects permit one to predict the stabilization of the 3(10)-helix with respect to the extended and 2(7)-ribbon conformations when the number of residues in the polypeptide chain increases. The interactions associated with the pi-electron density of the side chains can easily explain this finding. The effects of the solvent and the crystalline packing on the different conformations were modeled using a self-consistent reaction field (SCRF) method and a molecular mechanics approach to the packing, respectively. Both the aqueous and crystal environments seem to be a key factor in the stabilization of the helical conformation. Finally, the variations of electrostatic parameters such as atomic point charges and dipole moments in delta Ala-containing peptides with internal (conformation) and external (solvent) effects are discussed.

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环境的影响和pi-pi堆叠相互作用在脱氢丙氨酸寡肽中3(10)-螺旋构象稳定中的作用。
对脱氢丙氨酸(delta Ala)寡肽中延伸的2(7)带和3(10)螺旋构象的链长依赖性稳定性进行了量子力学研究。为了解决该研究,寡肽δ Ala(n),其中n从1到6变化,通过使用半经验AMI方法计算。协同自由能效应允许人们预测当多肽链中残基数量增加时,3(10)-螺旋相对于延伸构象和2(7)-带构象的稳定性。与侧链的电子密度相关的相互作用可以很容易地解释这一发现。采用自洽反应场(SCRF)方法和分子力学方法分别模拟了溶剂和晶体填料对不同构象的影响。水环境和晶体环境似乎都是螺旋构象稳定的关键因素。最后,讨论了含α - δ肽中原子点电荷和偶极矩等静电参数在内部(构象)和外部(溶剂)效应下的变化。
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