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Information × Registration Number 0226U001142, (0124U002143) , R & D reports Title Study of non-enzymatic activation of prothrombin popup.stage_title In silico пошук низькомолекулярних сполук, здатних взаємодіяти з активаційної «Ile16»-коміркою протромбіну. Дослідження здатності отриманих сполук активувати протромбін. Пошук сайтів взаємоії стафілокоагулази і протромбіну для пошуку додаткових регуляторних сайтів взаємодії. Head Ihor V. Komarov, Доктор хімічних наукChernyshenko Volodymyr O., Доктор біологічних наук Registration Date 21-01-2026 Organization Department for special training National academy of science of Ukraine at Kiev University popup.description1 The aim of the work is to study of non-enzymatic activation of prothrombin, as well as the search for peptides and/or low-molecular compounds that are potentially capable to activate prothrombin non-enzymatically. popup.description2 The subject of the research - non-enzymatic activation of prothrombin, wich consists in exposing the thrombin-like active center in the prothrombin molecule without proteolytic modification. А search for potential ligands of the activating "Ile16" cell of prothrombin was carried out using in silico methods. An additional series of peptides was synthesized, which, according to in silico data, are capable of interacting with the activation cell of prothrombin; the effect of the resulting peptides on the prothrombin activation process was tested. The chromogenic thrombin substrate S2238 was used to determine thrombin-like activity. To prove the complexation of the activator peptide with prothrombin, a fluorescent derivative of the most active activator peptide was synthesized. This peptide– contains an unnatural amino acid that accounts for ESIPT-mediated fluorescent properties. Chromatographic study showed resonance energy transfer in the prothrombin-activating peptide system with a fluorescent label, indicating their interaction. Experiments on the titration of prothrombin with a solution of this peptide were performed using a thermostated spectrofluorimeter cell at temperatures of 25 and 37 oC. In both temperature regimes, a significant decrease in the intrinsic fluorescence of prothrombin was recorded with each subsequent added volume of peptide, which indicates the sensitivity of the fluorescence spectroscopy method for recording intermolecular interactions in the prothrombin - peptide system under study. During the in silico study of low molecular weight compounds, their main characteristics were determined - the presence of a positively charged donor group that forms a salt bridge and hydrogen bonds with Asp194; the presence of hydrophobic groups, both cyclic and aliphatic, immersed in the Ile16 cell was also important. Тhe main results of the work are the discovery and synthesis of peptides that are capable of non-enzymatically activating prothrombin. Product Description popup.authors Oleksandr Y. Tsuvariev Oleksii O. Hrabovskyi Anastasiia O. Pavlenko Shevchenko Yeva V. Lypenko Oleksii S. Ilia Savchenko popup.nrat_date 2026-01-21 Close