Conformations of model peptides in membrane-mimetic environments.

Conformations of model peptides in membrane-mimetic environments.
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膜模拟环境中模型肽的构象。

DOI:
10.1016/s0006-3495(82)84676-6
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发表时间:
1982
影响因子:
3.4
通讯作者:
Watnick,PI
Watnick,PI
中科院分区:
生物学3区
文献类型:
--
作者:
Gierasch,LM;Lacy,JE;Thompson,KF;Rockwell,AL;Watnick,PI

文献摘要

被引文献

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通过对多种模拟膜介质中模型肽的研究,研究了膜环境对多肽链构象能量的影响。核磁共振(NMR)和圆二色性(CD)的数据得到了多肽在散装疏水溶剂,正常胶束和反胶束。研究了几种疏水多肽在十二烷基硫酸钠水溶液中的溶解作用。核磁共振和CD数据表明,胶束溶解肽经历了大量甲醇的构象影响环境,构象自由度降低。与胶束相互作用的肽的驻留位置似乎在表面活性剂头基团附近,在水渗透的区域,而不是在胶束核心。强亲水性多肽通过反胶束在非极性溶剂中被溶解。这些肽位于与表面活性剂的头部基团密切相关的小水池中。核磁共振和CD数据表明,该界面水区对多肽增溶物的构象影响不同于散装水区。
The influence of a membrane environment on the conformational energetics of a polypeptide chain has been investigated through studies of model peptides in a variety of membrane-mimetic media. Nuclear magnetic resonance (NMR) and circular dichroism (CD) data have been obtained for the peptides in bulk hydrophobic solvents, normal micelles, and reversed micelles. Several hydrophobic peptides which are sparingly soluble in water have been solubilized in aqueous sodium dodecyl sulfate (SDS) solution. NMR and CD data indicate that the micelle-solubilized peptides experience an environment with the conformational impact of bulk methanol, and have decreased conformational freedom. The site of residence of the peptides interacting with the micelles appears to be near the surfactant head groups, in a region permeated by water, and not in the micelle core. Strongly hydrophilic peptides have been solubilized in nonpolar solvents by reversed micelles. These peptides are located in small water pools in close association with the head groups of the surfactant. NMR and CD data show that there is a conformational impact of this interfacial water region on peptide solubilizates distinct from that of bulk water.