Association characteristics of amphiphilic .ALPHA.-helices connected by flexible links.
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概要
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Amphiphilic helical peptides interlinked with sequences bearing a flexible mobility were designed and synthesized. The sequences containing glycine and/or cystine were adopted for the linkage parts. The secondary structure of the peptides was investigated by circular dichroism(CD) and the super-secondary structure was estimated. The CD spectra and their pH dependence show that the peptides have almost the same α-helix contents as designed and that the helices associate to be "coiled-coil" at neutral pH. The apparent helix contents increase at low pH and some of helices are subject to denaturation at high pH. The denaturation of α-helix bundles by guanidine hydrochloride is contemplated to be three-state transition. It is proposed that the peptides construct α-helix bundles with both loose and tight contacts between helices. Two kinds of folded structure constructed with 2 or more helices are also suggested.
- 公益社団法人 日本化学会の論文
著者
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Ichimura Kunihiro
Research Center For Materials With Integrated Properties Toho University
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Morii Hisayuki
Research Institute for Polymers and Textiles
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Uedaira Hatsuho
Research Institute for Polymeres and Textiles
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Honda Shinya
Research Institute for Polymers and Textiles
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