Monoamine oxidases inhibitors from Colvillea racemosa: Isolation, biological evaluation, and computational study.

Autor: Mohamed EI; National Center for Natural Products Research, Research Institute of Pharmaceutical Sciences, School of Pharmacy, University of Mississippi, MS 38677, United States; Department of Pharmacognosy, Faculty of Pharmacy, Beni-Suef University, Beni-Suef 62514, Egypt., Zaki MA; National Center for Natural Products Research, Research Institute of Pharmaceutical Sciences, School of Pharmacy, University of Mississippi, MS 38677, United States; Department of Pharmacognosy, Faculty of Pharmacy, Beni-Suef University, Beni-Suef 62514, Egypt., Chaurasiya ND; National Center for Natural Products Research, Research Institute of Pharmaceutical Sciences, School of Pharmacy, University of Mississippi, MS 38677, United States., Owis AI; Department of Pharmacognosy, Faculty of Pharmacy, Beni-Suef University, Beni-Suef 62514, Egypt., AbouZid S; Department of Pharmacognosy, Faculty of Pharmacy, Beni-Suef University, Beni-Suef 62514, Egypt., Wang YH; National Center for Natural Products Research, Research Institute of Pharmaceutical Sciences, School of Pharmacy, University of Mississippi, MS 38677, United States., Avula B; National Center for Natural Products Research, Research Institute of Pharmaceutical Sciences, School of Pharmacy, University of Mississippi, MS 38677, United States., Seida AA; Department of Pharmacognosy, Faculty of Pharmacy, Cairo University, Cairo 11562, Egypt., Tekwani BL; National Center for Natural Products Research, Research Institute of Pharmaceutical Sciences, School of Pharmacy, University of Mississippi, MS 38677, United States; Department of BioMolecular Sciences, School of Pharmacy, University of Mississippi, MS 38677, United States. Electronic address: btekwani@olemiss.edu., Ross SA; National Center for Natural Products Research, Research Institute of Pharmaceutical Sciences, School of Pharmacy, University of Mississippi, MS 38677, United States; Department of BioMolecular Sciences, School of Pharmacy, University of Mississippi, MS 38677, United States. Electronic address: sross@olemiss.edu.
Jazyk: angličtina
Zdroj: Fitoterapia [Fitoterapia] 2018 Jan; Vol. 124, pp. 217-223. Date of Electronic Publication: 2017 Nov 14.
DOI: 10.1016/j.fitote.2017.11.009
Abstrakt: Bioassay-guided fractionation and chemical investigation of Colvillea racemosa stems led to identification of two new α, β-dihydroxydihydrochalcones, colveol A (1) and colveol B (2) along with fifteen known compounds. The structures were elucidated via interpretation of spectroscopic data. The absolute configurations of the dihydrochalcones 1 and 2 were assigned by a combination of chemical modification and electronic circular dichroism data. The isolated compounds were evaluated for their inhibition activity toward recombinant human monoamine oxidases (rhMAO-A and -B). Compound 1 demonstrated preferential inhibition against hMAO-A isoenzyme (IC 50 0.62μM, SI A/B 0.02) while S-naringenin (13) and isoliquiritigein (15) demonstrated preferential hMAO-B inhibition (IC 50 0.27 and 0.51μM, SI A/B 31.77 and 44.69, respectively). Fisetin (11) showed inhibition against hMAO-A with IC 50 value of 4.62μM and no inhibitory activity toward hMAO-B up to 100μM. Molecular docking studies for the most active compounds were conducted to demonstrate the putative binding modes. It suggested that 1 interacts with Gln215, Ala111, Phe352, and Phe208 amino acid residues which have a role in the orientation and stabilization of the inhibitor binding to hMAO-A, while S-naringenin (13) occupies both entrance and substrate cavities and interacts with Tyr326, a critical residue in inhibitor recognition in hMAO-B.
(Copyright © 2017. Published by Elsevier B.V.)
Databáze: MEDLINE
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