Docking studies on monoamine oxidase-B inhibitors: Estimation of inhibition constants (K-i) of a series of experimentally tested compounds

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Date

2005

Authors

Yelekçi, Kemal

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Pergamon-Elsevier Science Ltd

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Abstract

Monoamine oxidase (EC1.4.3.4
MAO) is a mitochondrial outer membrane flavoenzyme that catalyzes the oxidation of biogenic amines. It has two distinct isozymic forms designated MAO-A and MAO-B each displaying different substrate and inhibitor specificities. They are the well-known targets for antidepressant and neuroprotective drugs. Elucidation of the X-ray crystallographic structure of MAO-B has opened the way for molecular modeling studies. A series of experimentally tested (1-10) model compounds has been docked computationally to the active site of the MAO-B enzyme. The AutoDock 3.0.5 program was employed to perform automated molecular docking. The free energies of binding (Delta G) and inhibition constants (K-i) of the docked compounds were calculated by the Lamarckian Genetic Algorithm (LGA) of AutoDock 3.0.5. Excellent to good correlations between the calculated and experimental K-i values were obtained. (c) 2005 Elsevier Ltd. All rights reserved.

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Keywords

Docking, MAO-B inhibitors

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Citation

56

WoS Q

N/A

Scopus Q

Q2

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Volume

15

Issue

20

Start Page

4438

End Page

4446