Chemical Synthesis of Multiblock Copolypeptides Inspired by Spider Dragline Silk Proteins
Chemical Synthesis of Multiblock Copolypeptides Inspired by Spider Dragline Silk Proteins
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DOI：
10.1021/acsmacrolett.7b00006
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发表时间：
2017-02-01
影响因子：
7.015
通讯作者：
Numata, Keiji
中科院分区：
文献类型：
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作者：
Tsuchiya, Kousuke;Numata, Keiji
通过两步化学合成方法合成了新型多嵌段多肽，其结构与蜘蛛丝蛋白（蜘蛛蛋白）中观察到的独特序列相似，即使用木瓜蛋白酶进行化学酶聚合，然后进行后缩聚。通过化学酶聚合制备了两种类型的多肽片段：作为硬嵌段的聚丙氨酸，其在蜘蛛丝纤维中形成β-折叠，以及作为软嵌段的聚（甘氨酸-随机亮氨酸）。使用多磷酸作为缩合剂通过后缩聚连接这两个片段。广角X射线衍射（WAXD）和红外测量表明，所得多嵌段多肽形成反平行β-折叠结构，其结晶度与蜘蛛丝相似，从而形成纤维状形态。这项工作提供了模拟蜘蛛丝二级结构的合成多嵌段多肽的第一个例子。
Novel multiblock polypeptides with a structure similar to the unique sequence observed in spider silk proteins (spidroins) were synthesized via a two-step chemical synthesis method, that is, chemoenzymatic polymerization, using papain followed by postpolycondensation. Two types of polypeptide fragments were prepared by chemoenzymatic polymerization: polyalanine as a hard block, which forms beta-sheets in the spider silk fibers, and poly(glycine-random-leucine) as a soft block. These two fragments were ligated by postpolycondensation using polyphosphoric acid as a condensing agent. Wide-angle X-ray diffraction (WAXD) and IR measurements revealed that the resulting multiblock polypeptides formed an antiparallel beta-sheet structure with a degree of crystallinity similar to that of spider silk, which resulted in a fibrous morphology. This work provides the first example of a synthetic multiblock polypeptide mimicking the secondary structures of spider silk.