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Volume 8
Journal of Traditional Medicine & Clinical Naturopathy
Page 50
June 20-21, 2019 Dubai, UAE
Joint Meeting on
&
2
nd
World Congress on Traditional & Complemenatry Medicine
2
nd
International Conference on Herbal & Traditional Medicine
Traditional Med Meet 2019 &
Herbal Traditional 2019
June 20-21, 2019
Rana M Qasaymeh et al., J Tradit Med Clin Natur 2019, Volume 8
Predictive binding affinity of plant-derived natural products towards the protein
kinase G enzyme of
Mycobacterium tuberculosis
Rana M Qasaymeh, Dino Rotondo and Veronique Seidel
University of Strathclyde, UK
T
uberculosis (TB) caused by
Mycobacterium tuberculosis
is a growing public health concern worldwide,
especially with the emerging challenge of drug resistance to the current drugs. Efforts to discover and
develop some novel, more effective and safer anti-TB drugs are urgently needed. Products from natural
sources, such as medicinal plants have long played an important role in traditional medicine and continue to
provide some inspiring templates for the design of new drugs. Protein kinase G, produced by
M. tuberculosis
(MtPKnG), is a eukaryotic-like serine/threonine kinase that has been reported to prevent phagosome-
lysosome fusion and help prolong
M. tuberculosis
survival within the host’s macrophages. Here, we used
an in silico target-based approach (docking) to predict the interactions between MtPknG and 84 chemical
constituents from two medicinal plants (
Pelargonium reniforme and Pelargonium sidoides
) that have a well-
documented historical use as natural remedies for TB. Docking scores for ligands towards the target protein
were calculated using AutoDock Vina as the predicted binding free energies, with the lowest score indicating
the highest ligand/protein affinity. The scores obtained ranged between -5.8 and -13.2 kcal/mol. The flavonoid
derivatives (isoorientin 2”-O-gallate and isovitexin 2”-O-gallate) present in
P. reniforme/sidoides
aerial parts
displayed the best binding affinity towards MtPknG (-13.2 and -12.6 kcal/mol), with docking scores superior
to the control inhibitor AX20017 (-7.9 kcal/mol). The observation of the predictive binding affinity of these
natural products towards MtPknG warrants further in vitro investigations as they could represent some
chemical scaffolds for the design of new MtPknG inhibitors.
Biography
Rana M Qasaymeh is currently pursuing her PhD at the Starthclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde,
UK.
qwb17191@strath.ac.uk