Abstract
Objective: In the present study, a novel series of 1, 3, 4-thiadiazole derivatives were docked against the mycobacterium tuberculosis protein kinase G. 1, 3, 4–thiadiazole derivatives with a modified primary amine group at 5th position were used for docking studies.Methods: The three-dimensional structure of the protein was obtained from PDB, and its active sites were predicted. The structures of all the compounds were drawn using chemdraw software version 8.0. The docking studies were done by using schrödinger software against the enzyme protein kinase G. Totally eighteen compounds was synthesized based on glide scoreResults: In this Docking study the thiadiazole analogues were showing good binding energy. The amino acids residues GLU588, SER412, GLY410 and GLU 628 in the kinase domain active site form hydrogen bonds with the ligand.Conclusion: The compounds D34, D16, D7, D25, D15, and D27 showed better interaction with protein kinase G (pknG) more than the other drug molecules
Highlights
Mycobacterium tuberculosis (MTB) is an aerobic pathogenic bacteria and is the causative agent of most cases of tuberculosis
The ligand structures were constructed using the splinter dictionary of Maestro 9.4 (Schrodinger, LLC) using the Optimized Potentials for Liquid Simulations-All Atom (OPLS-AA) force field [7] with the steepest descent followed by curtailed Newton conjugate gradient protocol
The ligands are screened for their ability to dock within the active site of the enzyme
Summary
Mycobacterium tuberculosis (MTB) is an aerobic pathogenic bacteria and is the causative agent of most cases of tuberculosis. Tuberculosis (TB) is a lung infection and is highly contagious and deadly disease. The reason for the widespread of this disease is the emergence of multi-drug resistant TB strains and less availability of a new drug with a novel mechanism of action [1]. A permanent solution to this disease will be the development of vaccines. The most reliable will be chemotherapy, which requires effective and non-toxic antitubercular agents. The identification of new target sites will decrease the problems associated with multidrug resistant strains, for this biochemical pathway specific to the mycobacterium disease cycle must be better understood [2]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: International Journal of Pharmacy and Pharmaceutical Sciences
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
