Work

Phospha‐Michael Addition as a New Click Reaction for Protein Functionalization

Year: 2016

Type: article

Abstract: A new type of click reaction between an alkyl phosphine and acrylamide was developed and applied for site-specific protein labeling in vitro and in live cells. Acrylamide is a small electrophilic olefin that readily undergoes phospha-Michael addition with an alkyl phosphine. Our kinetic study indicated a second-order rate constant of 0.07 m(-1) s(-1) for the reaction between tris(2-carboxyethyl)phosphine and acrylamide at pH 7.4. To demonstrate its application in protein functionalization, we used a dansyl-phosphine conjugate to successfully label proteins that were site-specifically installed with N(ɛ) -acryloyl-l-lysine and employed a biotin-phosphine conjugate to selectively probe human proteins that were metabolically labeled with N-acryloyl-galactosamine.

Source: ChemBioChem

DOI: 10.1002/cbic.201500697

Authors: Yan‐Jiun Lee, Yadagiri Kurra, Wenshe R. Liu

Institution: Texas A&M University

Language: English

Topic: Click Chemistry and Applications

Subfield: Organic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: U.S. Public Health Service, National Cancer Institute

Awards: Phage Display with Two Genetically Incorporated Noncanonical Amino Acids, G2959989077