Correlation Engine 2.0
Clear Search sequence regions

Sizes of these terms reflect their relevance to your search.

Schistosomiasis is one of the neglected diseases causing considerable morbidity and mortality throughout the world. Microtubules with its main component, tubulin play a vital role in helminthes including schistosomes. Benzimidazoles represent potential drug candidates by binding β-tubulin. The study aimed to generate a homology model for the β-tubulin of S. mansoni using the crystal structure of O visaries (Sheep) β-tubulin (PDB ID: 3N2G D) as a template, then different β-tubulin models were generated and two previously reported benzimidazole derivatives (NBTP-F and NBTP-OH) were docked to the generated models, the binding results indicated that both S. mansoni, S. haematobium were susceptible to the two NBTP derivatives. Additionally, three mutated versions of S. mansoni β-tubulin wild-type were generated and the mutation (F185Y) seems to slightly enhance the ligand binding. Dynamics simulation experiments showed S. haematobium β-tubulin is highly susceptible to the tested compounds; similar to S. mansoni, moreover, mutated models of S. mansoni β-tubulin altered its NBTPs susceptibility. Moreover, additional seven new benzimidazole derivatives were synthesized and tested by molecular docking on the generated model binding site of S. mansoni β-tubulin and were found to have good interaction inside the pocket. Copyright © 2021 Elsevier B.V. All rights reserved.


Fouad El-Shehabi, Basem Mansour, Waleed A Bayoumi, Serry A El Bialy, Mohammad A Elmorsy, Hassan M Eisa, Amira Taman. Homology modelling, molecular dynamics simulation and docking evaluation of β-tubulin of Schistosoma mansoni. Biophysical chemistry. 2021 Nov;278:106660

Expand section icon Mesh Tags

Expand section icon Substances

PMID: 34482215

View Full Text