ANTIDEPRESSANT LIKE EFFECT OF NEWLY SYNTHESIZED COMPOUND 2[(N- BENZYLACETAMIDO) MERCAPTO] BENZIMIDAZOLE (VS 25) AND ITS POSSIBLE MECHANISM BY INHIBITION OF MONOAMINE OXIDASE ENZYME IN MICE

Abstract

Objective: The objective of the study was to investigate the antidepressant activity of a newly synthesized compound 2 [(N-benzylacetamido) mercapto] benzimidazole (VS 25) by forced swimming test in mouse and to explore the mechanism of action by its effect on monoamine oxidase enzyme in mouse brain.Methods: Swiss albino mice were randomly divided into 4 groups, each containing 6 animals. Group one was controlled and received 1 % cmc, p. o., Group II received moclobemide (50 mg/kg) p. o., group three and four received VS25 (30mg/kg and 60 mg/kg) once a day for 14 days.Results: In the forced swim test the decrease in immobility was 38.10% in moclobemide treated mice compared to 34.66% in VS25 (30 mg/kg) and 28.77% in VS 25 (60 mg/kg) treated mice. The percentage inhibition of the monoamine oxidase enzyme in mouse brain mitochondria was in moclobemide treated animals was 75.19% compared to 66.94% in VS 25 (30mg/kg) and 55.52% in VS 25 (60 mg/kg) treated animals. Moclobemide did not inhibit MAO B enzyme while VS25 (30 mg/kg) showed 6.48% and VS 25 (60 mg/kg) showed 4.75% inhibition.Conclusion: It is concluded that both moclobemide (50 mg/kg) and VS25 (30 mg/kg) showed antidepressant activity in mice. Moclobemide selectively inhibited MAO A enzyme in mouse brain. VS 25 (30 mg/kg) was equipotent as MAO A inhibitor but differed from moclobemide with respect to weak inhibition of MAO B activity also. 

Authors and Affiliations

Vaishali M. Mute, Subhash L. Bodhankar

Keywords

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  • EP ID EP579105
  • DOI -
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How To Cite

Vaishali M. Mute, Subhash L. Bodhankar (2015). ANTIDEPRESSANT LIKE EFFECT OF NEWLY SYNTHESIZED COMPOUND 2[(N- BENZYLACETAMIDO) MERCAPTO] BENZIMIDAZOLE (VS 25) AND ITS POSSIBLE MECHANISM BY INHIBITION OF MONOAMINE OXIDASE ENZYME IN MICE. International Journal of Pharmacy and Pharmaceutical Sciences, 7(2), 407-410. https://europub.co.uk./articles/-A-579105