Development of a series of cross-linking agents that effectively stabilize α-helical structures in various short peptides
Development of a series of cross-linking agents that effectively stabilize α-helical structures in various short peptides
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DOI：
10.1002/chem.200700843
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发表时间：
2008-01-01
影响因子：
4.3
通讯作者：
Inouye, Masahiko
中科院分区：
文献类型：
--
作者：
Fujimoto, Kazuhisa;Kajino, Masaoki;Inouye, Masahiko
设计了一系列不同刚性和长度的交联剂来稳定短肽的螺旋结构，并合成了这些交联剂。本研究中使用的短肽序列在i/i+4， i/i+71或i/i+11的位置上分别包含两个X残基（X=Dap, Dab， Orn和Lys），以提供交联的位点。将这些多肽与合成的交联剂进行反应，并通过圆二色性详细分析了所合成的交联多肽的螺旋含量。对于每一个肽类，我们发现了与交联剂的组合，适合在5℃下构建高达bb0 - 95%螺旋度的稳定螺旋结构。我们的方法也可以应用于天然蛋白(如Rev。
A series of cross-linking agents of varying rigidity and length were designed to stabilize helical structures in short peptides and were then synthesized. The sequences of the short peptides employed in this study each include two X residues (X=Dap, Dab, Orn, and Lys) at the i/i+4, i/i+71 or i/i+11 positions to provide the sites for cross-linking. These peptides were subjected to reaction with the synthesized cross-linking agents, and the helical content of the resulting cross-linked peptides were analyzed in detail by circular dichroism. For each of the peptide classes we found combinations with the cross-linking agents suitable for the construction of stable helical structures up to >95% helicity at 5 degrees C. Our method could also be applied to biologically related sequences seen in native proteins such as Rev.