INHIBITION OF FIBRIN POLYMERIZATION BY SYNTHETIC PEPTIDES CORRESPONDING TO Аα195-205 AND γ69-77 SITES OF FIBRIN MOLECULE T. A. Pozniak, L. P. Urvant, P. G. Gritsenko, V. I. Chernishov, N. A. Pydiura, E. V. Lugovskoi, S. V. Komisarenko

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Journal archive > 2014 > N 4 July-August

INHIBITION OF FIBRIN POLYMERIZATION BY SYNTHETIC PEPTIDES CORRESPONDING

TO Аα195-205 AND γ69-77 SITES OF FIBRIN MOLECULE

T. A. Pozniak, L. P. Urvant, P. G. Gritsenko, V. I. Chernishov, N. A. Pydiura, E. V. Lugovskoi, S. V. Komisarenko

Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;

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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 Аα195-205 specifically inhibited the stage of fibrin protofibril formation and peptide γ69-77 – the stage of fibrin 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.

Key words: sites of fibrin polymerization, peptides, inhibitors, proline brackets.

The original article in English is available for download in PDF format.