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Epi-croomine and croomine from Stemona tuberosa antimalarial drug for inhibiting dihydrofolate reductase (DHFR) activity and their molecular modeling

Journal Article


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Abstract


  • 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.

UOW Authors


  •   Pudjiastuti, Pratiwi (external author)
  •   Sumarsih, Sri (external author)
  •   Arwati, Heny (external author)
  •   Amalina, Ilma (external author)
  •   Fanani, Much Z. (external author)
  •   Utomo, Edi P. (external author)
  •   Fitri, Loeki E. (external author)
  •   Nugraha, Ari Satia (external author)
  •   Lie, Wilford
  •   Pyne, Stephen

Publication Date


  • 2014

Citation


  • Pudjiastuti, P., Sumarsih, S., Arwati, H., Amalina, I., Fanani, M. Z., Utomo, E. P., Fitri, L., Nugraha, A. S., Lie, W. & Pyne, S. G. (2014). Epi-croomine and croomine from Stemona tuberosa antimalarial drug for inhibiting dihydrofolate reductase (DHFR) activity and their molecular modeling. Journal of Chemical and Pharmaceutical Research, 6 (6), 544-548.

Scopus Eid


  • 2-s2.0-84924744506

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=2962&context=smhpapers

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/1944

Has Global Citation Frequency


Number Of Pages


  • 4

Start Page


  • 544

End Page


  • 548

Volume


  • 6

Issue


  • 6

Place Of Publication


  • India

Abstract


  • 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.

UOW Authors


  •   Pudjiastuti, Pratiwi (external author)
  •   Sumarsih, Sri (external author)
  •   Arwati, Heny (external author)
  •   Amalina, Ilma (external author)
  •   Fanani, Much Z. (external author)
  •   Utomo, Edi P. (external author)
  •   Fitri, Loeki E. (external author)
  •   Nugraha, Ari Satia (external author)
  •   Lie, Wilford
  •   Pyne, Stephen

Publication Date


  • 2014

Citation


  • Pudjiastuti, P., Sumarsih, S., Arwati, H., Amalina, I., Fanani, M. Z., Utomo, E. P., Fitri, L., Nugraha, A. S., Lie, W. & Pyne, S. G. (2014). Epi-croomine and croomine from Stemona tuberosa antimalarial drug for inhibiting dihydrofolate reductase (DHFR) activity and their molecular modeling. Journal of Chemical and Pharmaceutical Research, 6 (6), 544-548.

Scopus Eid


  • 2-s2.0-84924744506

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=2962&context=smhpapers

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/1944

Has Global Citation Frequency


Number Of Pages


  • 4

Start Page


  • 544

End Page


  • 548

Volume


  • 6

Issue


  • 6

Place Of Publication


  • India