Porous Peptide Complexes by a Folding-and-Assembly Strategy
Porous Peptide Complexes by a Folding-and-Assembly Strategy
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通过折叠和组装策略制备多孔肽复合物
DOI：
10.1002/asia.201700458
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发表时间：
2017
期刊：
影响因子：
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通讯作者：
Makoto Fujita
中科院分区：
文献类型：
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作者：
Tomohisa Sawada;Motoya Yamagami;Shuji Akinaga;Tatsuki Miyaji;Makoto Fujita
协调的折叠和组装过程是蛋白质自组装所必需的，但合成化学家很少尝试这种协调的策略。在这项工作中，我们通过配位驱动的折叠和组装策略创造了一种新的多孔多肽结构。通过AgNTf2与含有Gly- -Pro序列的三肽配体的络合，成功地获得了具有1.5Pro nm孔径的多孔骨架和PII螺旋多肽支架。以不同的方式修饰毛孔，保留了多肽配体的潜在PII螺旋构象。
Concerted folding and assembly processes are necessary for protein self‐assembly, yet such a concerted strategy has rarely been attempted by synthetic chemists. In this work, we have created a new porous peptide structure through a coordination‐driven folding‐and‐assembly strategy. A porous framework with 1.5 nm‐sized pores and a PIIhelical peptide scaffold was successfully obtained by complexation of AgNTf2and tripeptide ligands containing the Gly‐Pro‐Pro sequence. The pores were modified in various ways with retention of the latent PIIhelical conformation of the peptide ligand.