Bioanalitikai Intézet könyvtár
Credit: https://aok.pte.hu/hu/egyseg/160
Events
27 May 2024 10:34am
Invitation to the scientific lectures of Tamara Pajpanova and Ivan Bogdanov from the Bulgarian Academy of Sciences
We respectfully invite you and your colleagues to the seminar lectures to be held in the library of the Bioanalytical Institute on May 30 (Thursday) at 2:00 p.m.
Lecturers:
Prof. Tamara Pajpanova (Bulgarian Academy of Sciences - Sofia, and Neofit Rilski South-West University - Blagoevgrad, Bulgaria)
Title: "Why we focused our attention on the antimicrobial peptides?"
Ivan Bogdanov (PhD student, Institute of Molecular Biology, Bulgarian Academy of Sciences)
Title: "Structural insights of coagulation factor XIII as a promising therapeutic target in CVDs treatment"
Abstract:
In this study, High-ambiguity driven docking(a protein-protein docking approach) is performed to generate selected structures with the lowest intermolecular energies from the interactions between FXII-A2 and B2 subunits. In addition, structure-based drug design and molecular docking platform SeeSAR is used in order to analyse the interaction between FXIIIa and novel ligands. As a result, the binding affinities (including their physicochemical and drug-like properties) of the selected small molecules were estimated using SeeSAR “HYDE” (HYdrogen DEsolvation) algorithm.
Background: Cardiovascular diseases (CVDs) have the highest mortality rates (above 85% of the deaths caused are due to heart attacks and strokes) in the category of natural causes according to the World Health Organization(WHO). A way of preventing a fatal outcome is by fast treatment with anticoagulants to inhibit blood clotting factors. This affects the process of thrombosis by altering and preventing the formation of blood clots. FXIII is comprised of two dimeric-catalytic FXIII-A and two dimeric-regulatory FXIII-B subunits assembled in the blood plasma. After vascular injury, the FXIII activation peptide is cleaved by thrombin and along with calcium-mediated dissociation of the B subunits, FXIII is activated, which then covalently cross-links fibrin enhancing the blood clot stability. Inhibitors targeting blood clotting factor XIIIa (FXIIIa), involved in the last step of coagulation process are a promising target to develop a new generation of anticoagulants.