Abstract
Using the idea of "proline brackets" we have found four sites in fibrin amino acid sequence, and appropriate peptides were synthesized: γ69NPDESSKPN77, Bβ228QPDSSVKPY236, Bβ455RPFFPQ460 and Aα195LPSRDRQHLPL205. Turbidity and electron-microscopy analyses have demonstrated that synthetic peptide Aα195-205 specifically inhibited the stage of fibrin protofibril formation and peptide γ69-77 - the stage offibrin protofibril lateral association. The data obtained testify that there are the sites involved in these processes in the appropriate amino acid sequences of fibrin molecule.
Highlights
O n activation of the blood coagulation system thrombin is formed
There are data testifying to the existence of other functional sites participating in the fibrin polymerization process
The aim of this work is the localization of fibrin unknown functional sites, which participate in the process of its polymerization
Summary
O n activation of the blood coagulation system thrombin is formed This enzyme cleaves two fibrinopeptides А (FpА) from fibrinogen and transforms it into fibrin desА which is able to polymerize spontaneously by the intermolecular pairing of the complementary polymerization sites “А” and “а” [1, 2]. The sites of protein-protein interactions may be predicted in the presence of “proline brackets” [7] Basing on such approach, Budzynski et al [8] have presumed existence of fibrin polymerization site in the amino acid sequence Аα541-574, where the “proline bra cket” is located (Аα546-552). We have earlier locali zed the site of the fibrin polymerization in the fragment Bβ26APSLRPAPPPISGGGYRARPA46 [9] We have applied such approach in this work to preliminary localization of functionally important sites of fibrin molecule
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