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Original Articles Open Access
One of the mechanism actions of antimalarial drugsis by an inhibiting on the enzyme dihydrofolate reductase (DHFR), an enzyme target antifolate drug. Epi-croomine and croomine, are alkaloids isolated from Stemonatuberosa showed DHFR inhibition with Ki of 61.14 and 100.59 μM and KM values of30.68 and 27.06 μM at 10 ppm. The IC50 to the DHFR of croomine and pyrimethamine were 5.29 and 7.71 μM, respectively. Tuberostemonine is not active to the enzyme. The kinetic analysis showed that both epi-croomine and croomine competitively inhibited to the human DHFR recombinant. The molecular modeling of the compounds to the human DHFR was estimate depi-croomine and croomine’s binding free energy of -6.66 and -7.60 kcal/mol. The docking showed that both epi-croomine and croomine could possibly form hydrogen bonds with the amino acid residue of theAla9, which residues on the active site of the enzyme.
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Author(s): Pratiwi Pudjiastutia Sri Sumarsiha Heny Arwatib Ilma Amalinaa Much Z Fananic Edi P Utomod Loeki E Fitrie Ari S Nugrahafg Wilford Lieg and Stephen G Pyneg
malaria, epi-croomine, croomine, DHFR, Stemonatuberosa, antimalarial drug