Ursolic acid and carvacrol may be potential inhibitors of dormancy protein small heat shock protein16.3 of Mycobacterium tuberculosis.
Small heat shock protein16.3 (sHSP16.3) is a crucial protein for survival of Mycobacterium tuberculosis (MTB) in its host. Besides, this protein acts as a molecular chaperone during stress and is indispensable for MTB's growth, virulence and cell-wall thickening. sHSP16.3 is also a promising candidate for vaccine, serodiagnosis and drug design as well. In the present study, we have targeted sHSP16.3 with two phytochemicals, namely ursolic acid and carvacrol using in silico approach. Molecular docking analysis showed that both phytochemicals (ursolic acid and carvacrol) have docked with sHSP16.3 and shown tendency to inhibit the function of this vital protein of MTB. In addition, both compounds have exhibited strong compatibility with sHSP16.3 during whole 60 ns duration of molecular dynamics simulation. Further, the molecular mechanic/generalized Born/Poisson-Boltzmann surface area (MM/G/P/BSA) free energies were calculated which showed that both phytocompounds have stable and favourable binding energies causing strong binding with binding site of sHSP16.3. Taking together, the data of present study suggest that both phytocompounds may be potential inhibitor of sHSP16.3 of MTB and a best alternative to standard anti-tuberculosis drugs.
['Jee|Babban|B|', 'Kumar|Sanjay|S|', 'Yadav|Renu|R|', 'Singh|Yogesh|Y|', 'Kumar|Anuj|A|', 'Sharma|Naveen|N|']
D000995:Antitubercular Agents D001665:Binding Sites D000081007:Cymenes D006360:Heat-Shock Proteins D006801:Humans D018832:Molecular Chaperones D062105:Molecular Docking Simulation D056004:Molecular Dynamics Simulation D039821:Monoterpenes D009169:Mycobacterium tuberculosis D014315:Triterpenes D014376:Tuberculosis
ursolic acid carvacrol Mycobacterium tuberculosis sHSP16.3 in silico approach MD: Molecular dynamics MTB: Mycobacterium tuberculosis RMSD: Root-mean-square deviation TB: Tuberculosis sHSP16.3: Small heat shock protein16.3