title: Phospha-Michael Addition as a New Click Reaction for Protein Functionalization.
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.
authors.affiliation: Department of Chemistry, Texas A&M University, College Station, TX, 77843, USA.
authors.forename: Yan-Jiun
authors.initials: YJ
authors.lastname: Lee
authors.affiliation: Department of Chemistry, Texas A&M University, College Station, TX, 77843, USA.
authors.forename: Yadagiri
authors.initials: Y
authors.lastname: Kurra
authors.affiliation: Department of Chemistry, Texas A&M University, College Station, TX, 77843, USA. wliu@chem.tamu.edu.
authors.forename: Wenshe R
authors.identifier: http://orcid.org/0000-0002-7078-6534
authors.initials: WR
authors.lastname: Liu
mesh_terms: D020106:Acrylamide / Q000737:chemistry; D057930:Click Chemistry; D007700:Kinetics; D011506:Proteins / Q000737:chemistry*; D021241:Spectrometry, Mass, Electrospray Ionization
chemical_list: D011506:Proteins; D020106:Acrylamide
keywords: acrylamide; bioorthogonal reaction; click chemistry; phospha-Michael addition; phosphine