Novel polymeric membranes having chiral recognition sites converted from tripeptide derivatives

Citation
M. Yoshikawa et al., Novel polymeric membranes having chiral recognition sites converted from tripeptide derivatives, ANALYST, 126(6), 2001, pp. 775-780
Citations number
42
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Chemistry & Analysis","Spectroscopy /Instrumentation/Analytical Sciences
Journal title
ANALYST
ISSN journal
0003-2654 → ACNP
Volume
126
Issue
6
Year of publication
2001
Pages
775 - 780
Database
ISI
SICI code
0003-2654(2001)126:6<775:NPMHCR>2.0.ZU;2-0
Abstract
Six kinds of tripeptide derivative consisting of l-glutamic acid gamma -ben zyl ester [Glu(OBzl)] (E) and l-phenylalanine (Phe) (F), i.e. EEF, EFE, FEE , FEF, FFE and FFF, were converted into chiral recognition sites by adoptin g Boc-L-Trp as a print molecule. The formed chiral recognition sites discri minated between Ac-l-Trp and the corresponding D-isomer, and the l-isomer w as incorporated into the membrane in preference to the D-isomer. The affini ty constants between the recognition site formed in each membrane and Ac-l- Trp were determined to be 9.6 x 10(3) to 8.4 x 10(3) mol(-1) dm(3). The aff inity constant depends on both the tripeptide sequence and the amino acid r esidue content. Tripeptide derivatives containing more glutamic acid deriva tive residues or glutamic acid derivative as an amino-terminal residue show higher affinity constants.