The next seminar of the Institute for Physical Problems was held on 03.10.2019.

At the seminar, lead researcher of the Institute, Svetlana Demukhamedova has made a report on " Modeling of the interaction of  heme-soluble guanilaticyclase with carnosine".
The report describes on the theoretical modeling of the protein-ligand complex using the molecular docking method. Theoretical modeling by the molecular docking method allows one to obtain a set of ligand conformations optimally located at the receptor binding site and to predict the corresponding binding affinity. The docking procedure is very useful at the initial stage of development and creation of new drugs. The report details the AutoDockTools docking program and PyMol, a program for 3D visualization and analysis of ligand-enzyme interactions. In this study, the molecular docking of a carnosine inhibitor in the tautomeric form of N1H with the soluble guanylate cyclase enzyme (pdb 1xbn) was first performed. The biological properties of the carnosine dipeptide and the protein of soluble guanylate cyclase, the need for new drugs aimed at regulating the activity of the NO-sGC-cGMP system, and the reasons for choosing carnosine as an inhibitor inhibiting NO-dependent activation are described in detail. The results of the work show that the carnosine tautomer binds to the active center of guanylate cyclase, forming stable complexes with heme and amino acid residues and is characterized by binding affinity in the range from -4.6 to -2.1 kcal / mol for its various positions and conformations. The report considers the carnosine and heme poses obtained in docking against the background of the surrounding amino acid residues located in the active center of soluble guanylate cyclase. The distances formed as a result of the interaction between carnosine and heme atoms and nearby amino acid residues for stable binding positions are determined.

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