Papain-Catalyzed Chemoenzymatic Synthesis of Telechelic Polypeptides Using Bis(Leucine Ethyl Ester) Initiator.

Papain-Catalyzed Chemoenzymatic Synthesis of Telechelic Polypeptides Using Bis(Leucine Ethyl Ester) Initiator.
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使用双(亮氨酸乙酯)引发剂的木瓜蛋白酶催化化学酶合成遥爪多肽。

DOI:
10.1002/mabi.201600005
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发表时间:
2016
影响因子:
4.6
通讯作者:
K. Numata
K. Numata
中科院分区:
工程技术3区
文献类型:
--
作者:
K. Tsuchiya;K. Numata

文献摘要

被引文献

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为了构建独特的多肽结构,设计了一种新型的具有两个亮氨酸乙酯单元的遥爪型引发剂用于化学酶促聚合。甘氨酸或丙氨酸乙酯在引发剂存在下使用木瓜蛋白酶进行化学酶促聚合,并且在每个亮氨酸乙酯单元处发生增殖以产生遥爪多肽。遥爪多肽的形成通过(1)1H NMR和MALDI-TOF质谱确认。AFM观察表明,遥爪聚丙氨酸形成了长的纳米纤维,而聚合度相近的线性聚丙氨酸则呈现颗粒状结构。远螯聚甘氨酸和聚丙氨酸分别显示聚甘氨酸II和反平行β折叠的晶体结构。这表明,这种方法来合成遥爪型多肽可能开辟了一条途径,构建新的层次结构的自组装。
In order to construct unique polypeptide architectures, a novel telechelic-type initiator with two leucine ethyl ester units is designed for chemoenzymatic polymerization. Glycine or alanine ethyl ester is chemoenzymatically polymerized using papain in the presence of the initiator, and the propagation occurs at each leucine ethyl ester unit to produce the telechelic polypeptide. The formation of the telechelic polypeptides is confirmed by (1) H NMR and MALDI-TOF mass spectroscopies. It is revealed by AFM observation that long nanofibrils are formed from the telechelic polyalanine, whereas a conventional linear polyalanine with a similar degree of polymerization shows granule-like structures. The telechelic polyglycine and polyalanine show the crystalline structures of Polyglycine II and antiparallel β-sheet, respectively. It is demonstrated that this method to synthesize telechelic-type polypeptides potentially opens up a pathway to construct novel hierarchical structures by self-assembly.