Utilization of oxygen radicals by synthetic proline-rich oligopeptides

Inhibition of superoxide by two synthetic proline-rich hexapeptides simulating the hinge region of the IgG molecule has been studied. The CPPPEL (P-Cys) peptide was active in utilizing superoxide (O2.-), while the APPPEL (P-Ala) peptide had no such activity. Spontaneous formation of clusters with si...

Full description

Saved in:

Bibliographic Details
Published in:	Biokhimiia (Moscow, Russia) Vol. 57; no. 11; p. 1744
Main Authors:	Kul'berg, A Ia, Oranian, R R, Shibnev, B A
Format:	Journal Article
Language:	Russian
Published:	Russia (Federation) 01-11-1992
Subjects:	Catalysis Free Radicals Kinetics Oligopeptides - chemistry Oligopeptides - metabolism Oxygen - metabolism Proline - analysis
Online Access:	Get more information
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	Inhibition of superoxide by two synthetic proline-rich hexapeptides simulating the hinge region of the IgG molecule has been studied. The CPPPEL (P-Cys) peptide was active in utilizing superoxide (O2.-), while the APPPEL (P-Ala) peptide had no such activity. Spontaneous formation of clusters with six and/or eight monomers was shown for P-Cys, but not P-Ala. Preincubation of mixed P-Cys and P-Ala resulted in the appearance of a product with a high affinity for O2.-. Incubation of the mixture at 56 degrees C led to inactivation. Preincubation of P-Cys with ZnCl2 reversed the main pathway of O2.- utilization by P-Cys. The relationship of the P-Cys activity to its clusterization is discussed.
ISSN:	0320-9725