Site-specific protein transamination using N-methylpyridinium-4-carboxaldehyde.

ABSTRACT: The controlled attachment of synthetic groups to proteins is important for a number of fields, including therapeutics, where antibody-drug conjugates are an emerging area of biologic medicines. We have previously reported a site-specific protein modification method using a transamination reaction that chemoselectively oxidizes the N-terminal amine of a polypeptide chain to a ketone or an aldehyde group. The newly introduced carbonyl can be used for conjugation to a synthetic group in one location through the formation of an oxime or a hydrazone linkage. To expand the scope of this reaction, we have used a combinatorial peptide library screening platform as a method to explore new transamination reagents while simultaneously identifying their optimal N-terminal sequences. N-Methylpyridinium

SUBMITTER: Witus LS 

PROVIDER: S-EPMC4136391 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature