N-terminal protein modification through a biomimetic transamination reaction

ORGN 917

Rebecca A. Scheck, Department of Chemistry, University of California-Berkeley, 727 Latimer Hall, Berkeley, CA 94720
A convenient bioconjugation method has been developed for the selective introduction of ketone or aldehyde groups at the N-termini of proteins and peptides. This reaction utilizes the cofactor pyridoxal 5'-phosphate (PLP) to effect a biomimetic transamination product that can further derivitized through oxime formation. The mild conditions required for this transformation are conducive to maintaining the natural functionality of protein substrates. The scope of this reaction will be discussed for a variety of protein substrates, along with an account of some mechanistic aspects of this PLP-mediated transamination.
 

Proteins, Peptides, Amino Acids, and Enzyme Inhibitors
8:00 AM-12:00 PM, Thursday, August 23, 2007 BCEC -- 258B, Oral

Division of Organic Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007