期刊
BIOCONJUGATE CHEMISTRY
卷 27, 期 10, 页码 2260-2265出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.bioconjchem.6b00371
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- German Federal Ministry of Education and Research (BMBF) in the context of the German Center for Lung Research (DZL) [82DZL00101]
Sulfhydryl functions of thiol-containing amino acids are prime attachment sites for conjugation of labels, ligands, or drugs to proteinaceous compounds. Usually the thiol is offered a xenobiotic electrophilic moiety from the molecule to be attached such as a maleimido function. As sulfhydryls tend to oxidize into disulfides they must be reduced before conjugation. A popular thiol reduction reagent in biosciences is the substituted phosphine tris(2-carboxyethyl)phosphine (TCEP). Yet, phosphines are nucleophilic, too, and thus potentially compete with thiols for the electron-poor alkene moiety of maleimide resulting in complex product mixtures. To overcome this shortcoming we developed a method to eliminate excess reducing agent in the reaction mixture by selective oxidation of the phosphine with azidobenzoic acid before coupling. This results in a selective and efficient labeling of cysteines by maleimides.
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