Selectivity and stability of N-terminal targeting protein modification chemistries

被引：5

作者：

Barber, Lydia J. ^{[1
,2
,3
]}

Yates, Nicholas D. J. ^{[1
,2
]}

Fascione, Martin A. ^{[1
,2
]}

Parkin, Alison ^{[1
]}

Hemsworth, Glyn R. ^{[4
,5
]}

Genever, Paul G. ^{[2
,3
]}

Spicer, Christopher D. ^{[1
,2
,3
]}

机构：

[1] Univ York, Dept Chem, Heslington YO10 5DD, England

[2] Univ York, York Biomed Res Inst, Heslington YO10 5DD, England

[3] Univ York, Dept Biol, Heslington YO10 5DD, England

[4] Univ Leeds, Fac Biol Sci, Astbury Ctr Struct Mol Biol, Leeds LS2 9JT, England

[5] Univ Leeds, Fac Biol Sci, Sch Mol & Cellular Biol, Leeds LS2 9JT, England

来源：

RSC CHEMICAL BIOLOGY | 2023年 / 4卷 / 01期

基金：

英国工程与自然科学研究理事会; 英国生物技术与生命科学研究理事会;

关键词：

PEPTIDES;

D O I：

10.1039/d2cb00203e

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Protein N-termini provide uniquely reactive motifs for single site protein modification. Though a number of reactions have been developed to target this site, the selectivity, generality, and stability of the conjugates formed has not been studied. We have therefore undertaken a comprehensive comparative study of the most promising methods for N-terminal protein modification, and find that there is no 'one size fits all' approach, necessitating reagent screening for a particular protein or application. Moreover, we observed limited stability in all cases, leading to a need for continued innovation and development in the bioconjugation field.

引用

页码：56 / 64

页数：9

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