Alpha-chymotrypsin-catalyzed peptide synthesis using N-protected D-amino acid carbamoylmethyl esters as acyl donors.
Alpha-chymotrypsin-catalyzed peptide synthesis was carried out between an N-protected D-amino acid ester and an L-amino acid amide (acyl donor, 10 mM; acyl acceptor, 50 mM; enzyme, 2 mg ml(-1); pH 8). By using a highly reactive carbamoylmethyl (Cam) ester as acyl donor, the D-amino acid was incorporated into the N-terminus of the resulting dipeptide amide. N-Protected dipeptide amides bearing D-amino acids such as D-Phe, D-Leu and D-Ala at their N-terminus were synthesized in high yields (up to 80%) in 1-3 h.
Salam
Sayed Mohiuddin Abdus
SM
Department of Chemical Science and Technology, Faculty of Engineering, The University of Tokushima, 770-8506, Minamijosanjima, Tokushima, Japan.
Kagawa
Ken-Ichi
K
Kawashiro
Katsuhiro
K
D000596:Amino Acids / Q000737:chemistry*; D049148:Aminoacylation; D002384:Catalysis; D002918:Chymotrypsin / Q000737:chemistry*; D004579:Electron Transport; D004952:Esters; D010455:Peptides / Q000138:chemical synthesis*; D014867:Water / Q000737:chemistry*
D000596:Amino Acids; D004952:Esters; D010455:Peptides; D014867:Water; D002918:Chymotrypsin; C117608:alpha-chymotrypsin