Title

Structural insight into the binding of C60-derivatives with enoyl-pyruvate transferase from Helicobacter pylori

Authors

Mohammad Teimouri^1,*, Muhammad Junaid², Abbas Khan², Houjin Zhang¹

Affiliation

¹Department of Biochemistry, Huazhong University of science and Technology, China;

²Department of Bioinformatics and Biostatistics, Shanghai Jiao tong University, Shanghai, China.

Email

mmoh.teimouri@yahoo.com

Article Type

Hypothesis

Date

Received June 10, 2017; Revised June 12, 2017; Accepted June 25, 2017; Published June 30, 2017

Helicobacter pylori (H. pylori) is a human pathogen associated with acute gastritis and peptic ulcer. The MurA enzyme is an important drug target for the identification of ligands with improved efficacy and acceptable pharmaco-kinetic properties. We developed a homology model of H. Pylori MurA followed by refinement and molecular dynamics (MD) simulations. A total of 16 C60-derivatives were docked and its docking score were compared. Some of the known inhibitors were also similarly characterized and compared. Results show that five out of the sixteen C60-derivatives have good binding score. The MMPBSA analysis for the top five C60-derivatives shows good binding energy. This study reports the interaction patterns of selected C60 derivatives and MurA enzyme towards fullerene-based drug discovery.

Keywords

C60-derivatives, Helicobacter pylori, enoyl pyruvate transferase

Citation

Teimouri et al. Bioinformation 13(6): 185-191 (2017)

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.