Photo-control of helix content in a short peptide
Photo-control of helix content in a short peptide
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DOI：
10.1073/pnas.97.8.3803
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发表时间：
2000-04-11
影响因子：
11.1
通讯作者：
Woolley, GA
中科院分区：
文献类型：
--
作者：
Kumita, JR;Smart, OS;Woolley, GA
α-螺旋是广泛的肽和蛋白质中的关键结构元件。我们在这里报告的设计，合成和表征的改性肽，其中的螺旋内容可以可逆地photoregulated，该肽含有两个半胱氨酸残基，交联的偶氮苯衍生物在分子内的方式。根据该设计，偶氮苯交联剂从反式到顺式的光异构化导致肽在水中的螺旋含量大幅增加。
The alpha-helix is a key structural element in a wide range of peptides and proteins. We report here the design, synthesis, and characterization of a modified peptide in which the helix content can be reversibly photoregulated, The peptide contains two cysteine residues that are cross-linked by an azobenzene derivative in an intramolecular fashion. In accordance with the design, the photoisomerization of the azobenzene cross-linker from the trans to the cis form causes a large increase in the helix content of the peptide, in water.