Selective and reversible photochemical derivatization of cysteine residues in peptides and proteins

被引：65

作者：

Arumugam, Selvanathan ^{[1
]}

Guo, Jun ^{[2
]}

Mbua, Ngalle Eric ^{[2
]}

Friscourt, Frederic ^{[2
]}

Lin, Nannan ^{[1
]}

Nekongo, Emmanuel ^{[1
]}

Boons, Geert-Jan ^{[1
,2
]}

Popik, Vladimir V. ^{[1
]}

机构：

[1] Univ Georgia, Dept Chem, Athens, GA 30602 USA

[2] Univ Georgia, Complex Carbohydrate Res Ctr, Athens, GA 30602 USA

来源：

CHEMICAL SCIENCE | 2014年 / 5卷 / 04期

基金：

美国国家科学基金会; 美国国家卫生研究院;

关键词：

QUINONE METHIDE; CHEMICAL-MODIFICATION; THIOL; DISULFIDE; REACTIVITY; SULFHYDRYL; CHEMISTRY; ALBUMIN; GENERATION; ALCOHOLS;

D O I：

10.1039/c3sc51691a

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The selective derivatization of solvent-exposed cysteine residues in peptides and proteins is achieved by brief irradiation of an aqueous solution containing 3-(hydroxymethyl)-2-naphthol derivatives (NQMPs) with a 350 nm fluorescent lamp. NQMP can be conjugated with various moieties, such as PEG, dyes, carbohydrates, or possess a fragment for further selective derivatization, e. g., biotin, azide, alkyne, etc. Attractive features of this labeling approach include an exceptionally fast rate of the reaction and a requirement for a low equivalence of the reagent. The NQMP-thioether linkage is stable under ambient conditions, and survives protein digestion and MS analysis. Irradiation of an NQMP-labeled protein in a dilute solution (<40 mu M) or in the presence of a vinyl ether results in a traceless release of the substrate. The reversible biotinylation of bovine serum albumin, as well as the capture and release of this protein using NeutrAvidin Agarose resin beads has been demonstrated.

引用

页码：1591 / 1598

页数：8

共 53 条

[41] Assessment of temperature effects on β-aggregation of native and glycated albumin by FTIR spectroscopy and PAGE:: Relations between structural changes and antioxidant properties [J].