The importance of the glycosylation of antimicrobial peptides: natural and synthetic approaches

被引：104

作者：

Bednarska, Natalia G. ^{[1
]}

Wren, Brendan W. ^{[1
]}

Willcocks, Sam J. ^{[1
]}

机构：

[1] London Sch Hyg & Trop Med, Keppel St, London, England

来源：

DRUG DISCOVERY TODAY | 2017年 / 22卷 / 06期

基金：

英国生物技术与生命科学研究理事会;

关键词：

EOSINOPHIL CATIONIC PROTEIN; N-GLYCOSYLATION; POSTTRANSLATIONAL MODIFICATION; O-GLYCOSYLATION; HOST-DEFENSE; GLYCOPEPTIDE; MECHANISM; GLYCANS; CELLS; SITE;

D O I：

10.1016/j.drudis.2017.02.001

中图分类号：

R9 [药学];

学科分类号：

100702 [药剂学];

摘要：

Glycosylation is one of the most prevalent post-translational modifications of a protein, with a defining impact on its structure and function. Many of the proteins involved in the innate or adaptive immune response, including cytokines, chemokines, and antimicrobial peptides (AMPs), are glycosylated, contributing to their myriad activities. The current availability of synthetic coupling and glycoengineering technology makes it possible to customise the most beneficial glycan modifications for improved AMP stability, microbicidal potency, pathogen specificity, tissue or cell targeting, and immunomodulation.

引用

页码：919 / 926

页数：8

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