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通过蛋白酶催化的二肽寡聚化简化交替肽合成。

Simplifying alternating peptide synthesis by protease-catalyzed dipeptide oligomerization.

机构信息

Center for Biocatalysis and Bioprocessing of Macromolecules, Department of Chemical and Biomolecular Engineering, Polytechnic Institute of New York University, 6 Metrotech Center, Brooklyn, New York 11201, USA.

出版信息

Chem Commun (Camb). 2013 Jan 14;49(4):385-7. doi: 10.1039/c2cc36381j. Epub 2012 Nov 28.

DOI:10.1039/c2cc36381j
PMID:23190865
Abstract

A unique route to perfectly alternating oligopeptides is described. First, AG-OEt was prepared by standard chemical coupling. Then, AG-OEt was converted by papain-catalysis in 30 s to (AG)(x) (80%-yield, x = 9.4 ± 0.3). Extension of this strategy to other alternating peptide compositions as well as the importance of selecting a protease and reaction conditions that avoid competing transamidation and hydrolysis reactions is discussed.

摘要

本文描述了一种独特的方法来制备完美交替寡肽。首先,通过标准化学偶联制备了 AG-OEt。然后,AG-OEt 在木瓜蛋白酶的催化作用下在 30 秒内转化为(AG)(x)(产率为 80%,x = 9.4 ± 0.3)。讨论了将这种策略扩展到其他交替肽组成以及选择避免竞争转酰胺和水解反应的蛋白酶和反应条件的重要性。

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