Biomedical Research

All submissions of the EM system will be redirected to Online Manuscript Submission System. Authors are requested to submit articles directly to Online Manuscript Submission System of respective journal.
Reach Us +44 2038689735

Research Article - Biomedical Research (2017) Volume 28, Issue 20

Molecular docking analysis and determination of minimum inhibition concentration of VIM-38/R228S

Objective: The aim of this study was to determine the effects of residues at 228th positions of VIM-38 on minimum inhibition concentration (MIC) and molecular docking analysis.

Materials and Methods: blaVIM-38 gene was cloned into expression vector pET100/D-TOPO. Then pET100/D-TOPO-VIM-38 was used to generate the R228S mutation by site-directed mutagenesis. The mutant was transformed into E. coli Dh5α. Changes in the activity of mutation R228S was determined by E-test. Molecular docking analysis of the binding affinity of meropenem and imipenem with VIM-38 and VIM-38 R228S was performed using AutoDock Vina_1_1_2.

Results: According to E-test results, pET100/D-TOPO-VIM-38 and pET100/D-TOPO-VIM-38/ R228S have same MIC value for amoxicillin, ticarcillin/clavulanic acid, ampicillin and ticarcillin. It was determined decrease in pET100/D-TOPO-VIM-38/ R228S of MIC for aztreonam, amikacin and cefixine. There are 3-fold deference in MIC between pET100/D-TOPO-VIM-38 and pET100/D-TOPO-VIM-38/ R228S for cefoxitin. pET100/D-TOPO-VIM-38 has 0.5 μg/ml and pET100/D-TOPO-VIM-38/ R228S has 0.125 μg/m for imipenem, we observed 4-fold deference. Also, there is about 170-fold deference between pET100/D-TOPO-VIM-38 (16 μg/ml) and pET100/D-TOPO-VIM-38/ R228S (0.094 μg/ml) for meropenem. VIM-38 and VIM-38 R228S have very close to the negative low free energies of binding of the meropenem and imipenem.

Conclusion: These results showed that substitution (R228S) slightly have effect on enzyme activity.

Author(s): Azer Ozad Duzgun, Aysegul Saral

Abstract Full Text PDF

Get the App

best replica reviews