Abstract
A pentapeptide (EEAEN), which is the 24–28 fragment of the COOH-terminal sequence in the thymosinα1 molecule highly homologous with the 54–58 region of hirudin (with the complementary anion-binding exosite in the thrombin molecule), was synthesized by a solid-phase method. Preincubation of α-thrombin with EEAEN in concentrations of 0.1 pM to 1 nM reduced its clotting activity while preincubation of this enzyme with EEAEN in concentrations of 0.01 to 1 nM reduced its platelet-aggregating activity. The reaction of EEAEN with thrombin is shown to be similar to the reaction of the entire thymosinα1 molecule. It is concluded that the COOH-terminal thymosinα1 peptide EEAEN may be the reactive site responsible for the antithrombin activity of thymosinα1.
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Translated fromByulleten' Eksperimental'noi Biologii i Meditsiny, Vol. 120, No 7, pp. 26–29, July, 1995
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Strukova, S.M., Dugina, T.N., Samal', A.B. et al. Synthetic analog of the thymosinα1 fragment 24–28 alters the coagulating and aggregating activities of α-thrombin. Bull Exp Biol Med 120, 671–674 (1995). https://doi.org/10.1007/BF02444656
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DOI: https://doi.org/10.1007/BF02444656