[Effect of peptides--structural analogs of NH2-terminal sites of fibrin alpha- and beta-chains--on specific binding of the NH2-terminal disulfide bond of fibrin with fibrinogen].
Peptides Gly-Pro-Arg-Pro and Gly-His-Arg-Pro (fibrin alpha- and beta-chain NH2-terminal analogs, respectively) are studied for their effect on fibrinogen (F) and fibrin NH2-terminal disulphide knot (N-DSK) specific binding. Both peptides are found to inhibit the formation of soluble and insoluble F-N-DSK-complexes through inhibition of the interdomain D-E-binding. Gly-Pro-Arg-Pro is much more potent inhibitor than Gly-His-Arg-Pro. Lowering the insoluble F-N-DSK-copolymer quantity by concentration-dependent way these peptides do not change its composition described by the formula [F(N-DSK)2]n. Invariability of fibrinogen and N-DSK copolymer structure is asserted. In this structure neighbouring fibrinogen molecules are bound by two N-DSK molecules via the D1-E1 and D2-E2 binding sites.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002850:Chromatography, Gel; D004220:Disulfides; D005337:Fibrin / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism*; D066298:In Vitro Techniques; D009842:Oligopeptides / Q000494:pharmacology*; D011108:Polymers
D004220:Disulfides; D009842:Oligopeptides; D011108:Polymers; C048770:glycyl-histidyl-arginyl-proline; C034585:glycyl-prolyl-arginyl-proline; D005337:Fibrin; D005340:Fibrinogen
Vliianie peptidov--strukturnykh analogov NH2 kontsevykh uchastkov alpha- i beta-tsepeĭ fibrina--na spetsificheskoe sviazyvanie NH2-kontsevogo disul'fidnogo uzla fibrina s fibrinogenom.