New directions in glycoprotein engineering

被引：53

作者：

Macmillan, D

Bertozzi, CR ^{[1
]}

机构：

[1] Univ Calif Berkeley, Howard Hughes Med Inst, Dept Chem, Berkeley, CA 94720 USA

[2] Univ Calif Berkeley, Howard Hughes Med Inst, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

来源：

TETRAHEDRON | 2000年 / 56卷 / 48期

基金：

美国国家科学基金会;

关键词：

semisynthesis; glycoproteins; ligation;

D O I：

10.1016/S0040-4020(00)00836-X

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

Semisynthetic protein engineering techniques can be employed to overcome classic bottlenecks in the total synthesis or recombinant production of proteins bearing natural or unnatural post-translational modifications. Glycoproteins are particularly suited to semisynthesis as homogeneous samples for biological analyses are not readily available using traditional recombinant techniques. Here we report the use of expressed protein ligation for the construction of semi synthetic glycoproteins, which are assembled when recombinantly derived peptide alpha -thioesters are covalently joined with synthetic glycopeptides with clustered O-linked glycans by native chemical ligation. We demonstrate how this approach may be employed for the construction of glycoproteins bearing mucin-like domains. (C) 2000 Elsevier Science Ltd. All rights reserved.

引用

页码：9515 / 9525

页数：11

共 69 条

[21]

Hanessian S., 1997, PREPARATIVE CARBOHYD, P263

[22] Murine lymphotactin: Gene structure, post-translational modification and inhibition of expression by CD28 costimulation [J].