title: Peptide amidation by enzymatic transacylation and photolysis.
abstract: A series of model peptides with a C-terminal protected amide group were prepared by enzymatic transacylation. The protection groups were removed by photolysis to give the warranted peptide amides in high yields. Furthermore, fragments of human calcitonin were prepared. Various protective groups were employed, and the pH, solvent and concentration dependency of the enzymatic transcylation were examined. The photo-cleavage reaction was examined for wavelength, concentration and pH dependency. It was shown that the optimal yields required addition of a chemical scavenger for the photolysis byproducts.
authors.affiliation: Research Center for Medical Biotechnology, H.C. Orsted Institute, University of Copenhagen, Denmark.
authors.forename: D B
authors.initials: DB
authors.lastname: Henriksen
authors.forename: K
authors.initials: K
authors.lastname: Breddam
authors.forename: O
authors.initials: O
authors.lastname: Buchardt
mesh_terms: D000215:Acylation; D000577:Amides / Q000737:chemistry; D000595:Amino Acid Sequence; D002268:Carboxypeptidases / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008722:Methods; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010452:Peptide Biosynthesis; D010455:Peptides / Q000737:chemistry / Q000528:radiation effects; D010782:Photolysis
chemical_list: D000577:Amides; D010455:Peptides; D002268:Carboxypeptidases; C022633:serine carboxypeptidase