De novo design of orthogonal peptide pairs forming parallel coiled-coil heterodimers
De novo design of orthogonal peptide pairs forming parallel coiled-coil heterodimers
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DOI：
10.1002/psc.1331
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发表时间：
2011-02-01
影响因子：
2.1
通讯作者：
Jerala, Roman
中科院分区：
文献类型：
--
作者：
Gradisar, Helena;Jerala, Roman
我们使用卷曲螺旋片段的选择性和稳定性的原则来设计和实验测试一组四对平行卷曲螺旋形成肽组成的四个七肽重复。该设计是基于使用N-末端螺旋起始残基、静电和疏水相互作用基序的有利组合以及基于天冬酰胺残基掩埋的负设计基序来最大化所需对与最稳定的不需要的组合之间的稳定性差异。通过圆二色性（CD）对八种肽中的所有36对组合进行实验分析。基于CD光谱，每种肽仅与其设计的肽配偶体组合形成高水平的α-螺旋结构，这证明了设计的肽对组的正交性。版权所有（C）2010欧洲肽协会和约翰威利父子有限公司。
We used the principles governing the selectivity and stability of coiled-coil segments to design and experimentally test a set of four pairs of parallel coiled-coil-forming peptides composed of four heptad repeats. The design was based on maximizing the difference in stability between desired pairs and the most stable unwanted combinations using N-terminal helix initiator residues, favorable combinations of the electrostatic and hydrophobic interaction motifs and negative design motif based on burial of asparagine residues. Experimental analysis of all 36 pair combinations among the eight peptides was performed by circular dichroism (CD). On the basis of CD spectra, each peptide formed a high level of alpha-helical structure exclusively in combination with its designed peptide partner which demonstrates the orthogonality of the designed peptide pair set. Copyright (C) 2010 European Peptide Society and John Wiley & Sons, Ltd.