Peptide synthesis catalyzed by an antibody containing a binding site for variable amino acids

Ralph Hirschmann, Amos B. Smith, Carol M. Taylor, Patricia A. Benkovic, Scott D. Taylor, Kraig M. Yager, Paul A. Sprengeler, Stephen J. Benkovic

Research output: Contribution to journalArticlepeer-review

393 Scopus citations

Abstract

Monoclonal antibodies, induced with a phosphonate diester hapten, catalyzed the coupling of p-nitrophenyl esters of N-acetyl valine, leucine, and phenylalanine with tryptophan amid to form the corresponding dipeptides. All possible stereoisomeric combinations of the ester and amide substrates were coupled at comparable rates. The antibodies did not catalyze the hydrolysis of the dipeptide product nor hydrolysis or racemization of the activate esters. The yields of the dipeptides ranged from 44 to 94 percent. The antibodies were capable of multiple turnovers at rates that exceeded the rate of spontaneous ester hydrolysis. This achievement suggests routes toward creating a small number of antibody catalysts for polypeptide syntheses.

Original languageEnglish (US)
Pages (from-to)234-237
Number of pages4
JournalScience
Volume265
Issue number5169
DOIs
StatePublished - Jul 8 1994

All Science Journal Classification (ASJC) codes

  • General

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