Jayanthi S

Department of Biotechnology

School of Bio Sciences and Technology

Vellore Campus

Mathew B

Baek SC

Thomas Parambi DG

Lee JP

Mathew GE

Vinod D

Rapheal C

Devikrishna V

Kondarath SS

Vellore Institute of Technology (VIT) is a private university located in&nbsp;Tamil Nadu, India. Founded in 1984, as Vellore Engineering College, the institution offers 20 undergraduate, 34 postgraduate, four integrated and four research programs. It has campuses in Vellore, Amravati, Bhopal and Chennai.

VIT is one of the top ranked private universities in India according to NIRF, THE and QS Rankings.&nbsp;Govt. of India has recognized&nbsp;VIT, Vellore as an&nbsp;Institution of Eminence. This has allowed VIT to take independent quality initiatives and move up in world ranking.

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VIT University

Archiv der Pharmazie

In the present study, series of eleven (2E)-1-[4-(1H-imidazol-1-yl)substituted phenyl]-3-phenylprop-2-en-1-one (IM1-IM11) derivatives were synthesized and evaluated as inhibitors of recombinant human monoamine oxidase (MAO) A and B. The results indicate that (2E)-3-[4-(dimethylamino) phenyl]-1-[4-(1H-imidazol-1-yl) phenyl] prop-2-en-1-one (IM5) is a nonselective and reversible competitive inhibitor of MAO-A and MAO-B with IC50 values of 0.30 ± 0.010 and 0.40 ± 0.017 μM, respectively ; those of (2E)-1-[4-(1H-imidazol-1-yl) phenyl]-3-(4-methylphenyl) prop-2-en-1-one (IM4) were 1.06 ± 0.090 and 0.32 ± 0.021 μM, respectively. Kinetic studies document that both IM5 and IM4 are competitive inhibitors of MAO-A and MAO-B with Ki value of 0.11 ± 0.0085 and 0.085 ± 0.0064 μM, respectively. Molecular docking studies of lead compounds further explained the binding modes in the inhibitor binding cavity of both MAO-A and MAO-B.

Biomedicine & Pharmacotherapy

Imidazole bearing chalcones as a new class of monoamine oxidase inhibitors

A series of 11 indole-based chalcones (IC1–11) with various electron donating and withdrawing groups at the para position of the phenyl ring B were synthesized. All the compounds were tested for their human monoamine oxidase (hMAO)-A and hMAO-B inhibitory potencies. Most of the synthesized candidates proved to be potent and selective inhibitors of MAO-B rather than MAO-A, with a reversible and competitive mode. Among them, compound IC9 was found to be a potent inhibitor of hMAO-B with Ki = 0.01 ± 0.005 μM and a selectivity index of 120. It was found to be better than the standard drug, selegiline (hMAO-B with Ki = 0.20 ± 0.020 μM) with a selectivity index of 30.55. PAMPA assays were carried out for all the compounds in order to evaluate the capacity of the compounds to cross the blood–brain barrier. Moreover, the most potent MAO-B inhibitor, IC9, was nontoxic at 5 and 25 μM, with 95.20 and 69.17% viable cells, respectively. The lead compound IC9 has an antioxidant property of 1.18 Trolox equivalents by ABTS assay. Molecular modeling studies were performed against hMAO-B to observe binding site interactions of the lead compound. © 2016 WILEY-VCH Verlag GmbH &amp; Co. KGaA, Weinheim

Identification of Indole-Based Chalcones: Discovery of a Potent, Selective, and Reversible Class of MAO-B Inhibitors

Clinical and Translational Medicine

A perspective on multi‐target drug discovery and design for complex diseases

International Journal of Biological Macromolecules

Discovery of potent and reversible MAO-B inhibitors as furanochalcones

Bioorganic & Medicinal Chemistry Letters

Selective inhibition of monoamine oxidase A by hispidol

Potent and highly selective dual‐targeting monoamine oxidase‐B inhibitors: Fluorinated chalcones of morpholine versus imidazole

Journal	Data powered by TypesetArchiv der Pharmazie
Publisher	Data powered by TypesetWiley
ISSN	0365-6233
Open Access	0