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1-Methyl-2-undecyl-4(1H)-quinolone as an Irreversible and Selective Inhibitor of Type B Monoamine Oxidase

Year: 2003

Type: article

Abstract: The inhibitory compound of monoamine oxidase (MAO) activity was isolated from the CH(2)Cl(2) fraction of the fructus of Evodia rutaecarpa and identified as 1-methyl-2-undecyl-4(1H)-quinolone (1). Compound 1 showed a selective inhibition of type B MAO (MAO-B) activity with the IC(50) value of 15.3 microM using a substrate kynuramine, but did not inhibit type A MAO (MAO-A) activity. The kinetic analysis using Lineweaver-Burk plots indicated that compound 1 competitively inhibited MAO-B activity with the K(i) value of 9.91 microM. The inhibition of MAO-B by compound 1 was found to be irreversible by dialysis of the incubation mixture. These results suggest that compound 1 is a potent irreversible inhibitor of MAO-B, and may regulate catecholamine content in the neurons.

Source: Chemical and Pharmaceutical Bulletin

DOI: 10.1248/cpb.51.409

Authors: Myung Koo Lee, Bang Yeon Hwang, Seon A Lee, Gab Jin Oh, Woo Hoi Choi, Seong Su Hong, Kyong Soon Lee, Jai Seup Ro

Institutions: Chungbuk National University, University of Illinois Chicago, Samjin Pharm (South Korea)

Language: English

Topic: Bioactive natural compounds

Subfield: Drug Discovery

Field: Pharmacology, Toxicology and Pharmaceutics

Domain: Life Sciences

Open Access status: bronze

OpenAlex ID: W2136242567

FWCI: 0.686

Cites: 25

Cited by: 41

Related to: 10