Premium
Chiral recognition ability of oligopeptide derivatives consisting of glutamyl residues
Author(s) -
Yoshikawa Masakazu,
Nagai Yasuharu,
Moriguchi Koji,
Hiraoka Satoshi
Publication year - 2005
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.21307
Subject(s) - tetrapeptide , oligopeptide , residue (chemistry) , stereochemistry , amino acid , chemistry , peptide , amino acid residue , organic chemistry , peptide sequence , biochemistry , gene
The effect of the constituting amino acid residue [Glu(OBzl)] number on the chiral recognition ability was investigated. Chiral recognition sites were prepared from oligopeptide derivatives (constituting amino acid residue number = three–five) by adopting alternative molecular imprinting. It was made clear that with a constituting amino acid residue number of four, the tetrapeptide derivative of Glu(OBzl) is the best candidate material to generate a chiral recognition site among eight types of oligopeptide derivatives in the study. The affinity constant between Ac‐ L ‐Trp and a chiral recognition site ranged from 3.4 × 10 3 to 1.08 × 10 4 mol −1 dm 3 , depending on the number of Glu(OBzl) residues in an oligopeptide derivative. © 2005 Wiley Periodicals, Inc. J Appl Polym Sci 95: 1302–1309, 2005