Lindner W, Robey F A
Center for Drugs and Biologics, Food and Drug Administration, Bethesda, Maryland.
Int J Pept Protein Res. 1987 Dec;30(6):794-800. doi: 10.1111/j.1399-3011.1987.tb03388.x.
A method to incorporate N-chloroacetyl moieties at the amino termini of synthetic peptides using a standard program with an automated peptide synthesizer has been developed. The N-chloroacetyl-modified peptides react well with sulfhydryl containing proteins such as 4-mercaptobutyrimide-modified bovine serum albumin to form stable protein-peptide conjugates. By incorporating cysteine into the synthetic peptide, autopolymerization or cyclization of the synthetic peptide occurs by reaction of the free sulfhydryl with the chloroacetyl group. N-Chloroacetyl-derivatized peptides may be useful as reagents for potential peptide immunogens and vaccines.
