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Co‐oligopeptides of aromatic amino acids and glycine with variable distance between the aromatic residues. VII. Enzymatic synthesis of N‐protected peptide amides
Author(s) -
Saltman Robert,
Vlach Dagmar,
Luisi Pier Luigi
Publication year - 1977
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1977.360160312
Subject(s) - chemistry , residue (chemistry) , peptide , hydrolysis , oligopeptide , aromatic amino acids , coupling reaction , amino acid , glycine , amide , stereochemistry , catalysis , enzyme , organic chemistry , combinatorial chemistry , biochemistry
Several N‐protected peptide amides, containing two aromatic residues spaced by one glycyl residue, have been enzymatically synthesized starting from P‐Ar‐OH and H‐Gly‐Ar‐NH 2 (P is the protecting group and Ar is the aromatic residue) and using α‐chymotrypsin as the catalyst for the coupling step. Reactions have been carried out in water solution, at room temperature, and afford yields ranging between 20 and 75% ca. This coupling reaction occurs in a much more restricted set of conditions than the hydrolysis reaction, e.g., only within a small pH range (ca. 6.5–7.5) and with particular buffering agents. The advantages and limitations of this type of reaction, compared with conventional coupling procedures, are discussed.