Phospha-Michael Addition as a New Click Reaction for Protein Functionalization. Academic 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 0.07m(-1) s(-1) for the reaction between tris(2-carboxyethyl)phosphine and acrylamide at pH7.4. To demonstrate its application in protein functionalization, we used a dansyl-phosphine conjugate to successfully label proteins that were site-specifically installed with N() -acryloyl-l-lysine and employed a biotin-phosphine conjugate to selectively probe human proteins that were metabolically labeled with N-acryloyl-galactosamine.

authors

• Liu, Wenshe

published proceedings

• Chembiochem

altmetric score

• 1

author list (cited authors)

• Lee, Y., Kurra, Y., & Liu, W. R.

citation count

• 26

complete list of authors

• Lee, Yan-Jiun||Kurra, Yadagiri||Liu, Wenshe R

publication date

• March 2016

publisher

• Wiley  Publisher

published in

• ChemBioChem  Journal

keywords

• Acrylamide
• Bioorthogonal Reaction
• Click Chemistry
• Kinetics
• Phospha-michael Addition
• Phosphine
• Proteins
• Spectrometry, Mass, Electrospray Ionization

PubMed Central ID

• 26756316

Digital Object Identifier (DOI)

• 10.1002/cbic.201500697

start page

• 456

end page

• 461

volume

• 17

issue

• 6

URL

• http%3A%2F%2Fdx.doi.org%2F10.1002%2Fcbic.201500697