Novel polymeric membranes having chiral recognition sites converted from tripeptide derivatives

Yoshikawa, M Shimada, A Izumi, J

M. Yoshikawa et al., Novel polymeric membranes having chiral recognition sites converted from tripeptide derivatives, ANALYST, 126(6), 2001, pp. 775-780

42

INGLESE

Article

Chemistry & Analysis","Spectroscopy /Instrumentation/Analytical Sciences

ANALYST

0003-2654 → ACNP

126

6

2001

775 - 780

ISI

0003-2654(2001)126:6<775:NPMHCR>2.0.ZU;2-0

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.