[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 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.
Kul'berg
A Ia
AIa
Oranian
R R
RR
Shibnev
B A
BA
D002384:Catalysis; D005609:Free Radicals; D007700:Kinetics; D009842:Oligopeptides / Q000737:chemistry / Q000378:metabolism*; D010100:Oxygen / Q000378:metabolism*; D011392:Proline / Q000032:analysis*
D005609:Free Radicals; D009842:Oligopeptides; D011392:Proline; D010100:Oxygen
Utilizatsiia radikalov kisloroda sinteticheskimi prolin-bogatymi oligopeptidami.