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在配位驱动下,短肽折叠组装成类似蛋白质的两纳米大小的通道。

Coordination-driven folding and assembly of a short peptide into a protein-like two-nanometer-sized channel.

机构信息

Department of Applied Chemistry, School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656 (Japan).

出版信息

Angew Chem Int Ed Engl. 2014 Jul 7;53(28):7228-32. doi: 10.1002/anie.201403506. Epub 2014 May 23.

Abstract

Short peptide helices have attracted attention as suitable building blocks for soft functional materials, but they are rarely seen in crystalline materials. A new artificial nanoassembly of short peptide helices in the crystalline state is presented in which peptide helices are arranged three-dimensionally by metal coordination. The folding and assembly processes of a short peptide ligand containing the Gly-Pro-Pro sequence were induced by silver(I) coordination in aqueous alcohol, and gave rise to a single crystal composed of polyproline II helices. Crystallographic studies revealed that this material possesses two types of unique helical nanochannel; the larger channel measures more than 2 nm in diameter. Guest uptake properties were investigated by soaking the crystals in polar solutions of guest molecules; anions, organic chiral molecules, and bio-oligomers are effectively encapsulated by this peptide-folded porous crystal, with moderate to high chiral recognition for chiral molecules.

摘要

短肽螺旋因其适合作为构建软功能材料的结构单元而受到关注,但在结晶材料中却很少见。本文报道了一种新的短肽螺旋在结晶状态下的人工纳米组装体,其中肽螺旋通过金属配位进行三维排列。含有甘氨酸-脯氨酸-脯氨酸序列的短肽配体在水醇溶液中通过银(I)配位诱导其折叠和组装,得到由聚脯氨酸 II 螺旋组成的单晶。晶体结构研究表明,该材料具有两种独特的螺旋纳米通道,较大的通道直径超过 2nm。通过将晶体浸泡在极性客体分子溶液中研究了客体的摄入性质,阴离子、有机手性分子和生物低聚物可以被这种肽折叠多孔晶体有效包裹,对手性分子具有中等至高度的手性识别。

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