Mild and chemoselective peptide-bond cleavage of peptides and proteins at azido homoalanine

被引：23

作者：

Back, JW

David, O

Kramer, G

Masson, G

Kasper, PT

de Koning, LJ

de Jong, L

van Maarseveen, JH

de Koster, CG

机构：

[1] Univ Amsterdam, Mass Spectrometry Grp, Swammerdam Inst Life Sci, NL-1018 WV Amsterdam, Netherlands

[2] Ecole Normale Super, Lab Photochim & Photophys Supramol & Macromol, F-94235 Cachan, France

[3] Univ Amsterdam, Dept Organ Chem, Vant Hoff Inst Mol Sci, NL-1018 WS Amsterdam, Netherlands

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2005年 / 44卷 / 48期

关键词：

azides; nucleophilic substitution; phosphanes; proteolysis; triazenes;

D O I：

10.1002/anie.200502431

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Chemical Equation Presented) A gentle break: Cleavage of peptides containing the non-natural but proteogenic amino acid azido homoalanine can be accomplished by phosphine- or dithiol-mediated reductive activation of the azide functionality in aqueous buffers (see scheme). The resulting C-terminal lactone of one peptide fragment allows facile further derivatization. © 2005; Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：7946 / 7950

页数：5

共 31 条

[1] A strain-promoted [3+2] azide-alkyne cycloaddition for covalent modification of blomolecules in living systems [J].