Open AccessAssessment of structural peculiarities of glaziovianin A interaction with human α-, β and γ-tubulins
Author(s) -
П. А. Карпов,
S. I. Spivak,
O. V. Rayevsky,
O. Yu. Nyporko,
S. P. Ozheredov,
Ya. B. Blume
Publication year - 2018
Publication title -
faktori eksperimentalʹnoï evolûcìï organìzmìv
Language(s) - English
Resource type - Journals
eISSN - 2415-3826
pISSN - 2219-3782
DOI - 10.7124/feeo.v22.972
Subject(s) - tubulin , docking (animal) , molecular dynamics , ligand (biochemistry) , chemistry , binding site , gtp' , microtubule , molecular model , biophysics , stereochemistry , biochemistry , biology , computational chemistry , receptor , microbiology and biotechnology , medicine , nursing , enzyme
Aim. To determine the features of the ligand-protein interaction of glaziovianin A and human α-, β- and γ-tubulin. Methods. Protein and ligand spatial structure modelling (I-Tasser, Grid), molecular docking (CCDC Gold), molecular dynamics simulation (GROMACS). Results. Using the method of molecular docking in CCDC Gold ligand-protein complexes of glaziovianin A and human α-, β- and γ-tubulin were reconstructed. Studied ligand interactions in GTP/GDP-exchange and colchicine binding sites of different tubulin isotypes. The built ligand-protein complexes were studied using molecular dynamics simulations. Conclusions. Binding of glaziovianin A with human tubulin was confirmed exposing its derivatives as perspective tubulin effectors. The binding energies of ligand-protein interaction confirm higher affinity for β-tubulin molecules, and it was suggested that glazovianin A binding may occur at two alternative sites: GTP/GDP-exchange site and site of colchicine binding.
Keywords: tubulin, glaziovianin A, binding, antitumor activity.