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Pyrazoline: a promising scaffold for the inhibition of monoamine oxidase.

Publication Type : Journal Article

Publisher : Cent Nerv Syst Agents Med Chem

Source : Cent Nerv Syst Agents Med Chem, Volume 13, Issue 3, p.195-206 (2013)

Url :,the%20inhibition%20of%20Monoamine%20oxidase.&text=We%20propose%20that%20the%20selectivity,3%20position%20of%20the%20scaffold.

Keywords : Animals, Humans, Isoenzymes, Molecular Conformation, Monoamine oxidase, Monoamine Oxidase Inhibitors, Pyrazoles, Structure-Activity Relationship

Campus : Kochi

School : School of Pharmacy

Department : Pharmaceutical Chemistry & Analysis

Year : 2013

Abstract : In the five membered nitrogen containing heterocyclic family, pyrazoline could be recognized as a promising scaffold for the inhibition of Monoamine oxidase. Substitution at 1, 3 and 5-position of the pyrazoline nucleus displayed a significant activity towards MAO in the past 15 years. Our study identified the detailed structure activity relationship, the structural requirement for enzyme interaction and the effect of chirality on the pyrazoline nucleus towards MAO-A and MAO-B. We propose that the selectivity of pyrazoline nucleus towards MAO isoenzyme depends up on the bulkiness of the ring in the 1 and 3 position of the scaffold. The current review revealed that the derivatives of pyrazolines have proven to be versatile pharmacophores for the inhibition of MAO on the basis of existing literatures between (1998-2013).

Cite this Research Publication : Bijo Mathew, Suresh, J., Anbazhagan, S., and Mathew, G. Elizabeth, “Pyrazoline: a promising scaffold for the inhibition of monoamine oxidase.”, Cent Nerv Syst Agents Med Chem, vol. 13, no. 3, pp. 195-206, 2013.

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