Exploration of a library of piperonylic acid-derived hydrazones possessing variable aryl functionalities as potent dual cholinesterase and monoamine oxidase inhibitors.

V Pavan Kumar, M S Vishnu, Sandeep Kumar, Shivani Jaiswal, Senthil Raja Ayyannan

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Article in Molecular diversity, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 authors at 2 institutions in 1 country.

V Pavan KumarPharmaceutical Chemistry Research Laboratory II, Department of Pharmaceutical Engineering & Technology, Indian Institute of Technology (Banaras Hindu University), Varanasi, UP, 221005, India.ORCID http://orcid.org/0000-0001-8554-8232

M S VishnuPharmaceutical Chemistry Research Laboratory II, Department of Pharmaceutical Engineering & Technology, Indian Institute of Technology (Banaras Hindu University), Varanasi, UP, 221005, India.ORCID http://orcid.org/0000-0002-9661-1927

Sandeep KumarPharmaceutical Chemistry Research Laboratory II, Department of Pharmaceutical Engineering & Technology, Indian Institute of Technology (Banaras Hindu University), Varanasi, UP, 221005, India.ORCID http://orcid.org/0000-0002-0826-6546

Shivani JaiswalPharmaceutical Chemistry Research Laboratory II, Department of Pharmaceutical Engineering & Technology, Indian Institute of Technology (Banaras Hindu University), Varanasi, UP, 221005, India.ORCID http://orcid.org/0000-0001-6241-5082

Senthil Raja AyyannanPharmaceutical Chemistry Research Laboratory II, Department of Pharmaceutical Engineering & Technology, Indian Institute of Technology (Banaras Hindu University), Varanasi, UP, 221005, India. asraja.phe@iitbhu.ac.in.ORCID http://orcid.org/0000-0002-6008-4571

Indian Institute of Technology Indore · INIndian Institute of Technology BHU · IN

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6 · The paper itself

Abstract

A library of piperonylic acid-derived hydrazones possessing variable aryl moiety was synthesized and investigated for their multifunctional properties against cholinesterases (ChEs) and monoamine oxidases (MAOs). The in vitro enzymatic assay results revealed that the tested hydrazones have exhibited excellent cholinesterase inhibition profile. Compound 4i, (E)-N'-(2,3-dichlorobenzylidene)benzo[d][1,3]dioxole-5-carbohydrazide showed promising dual inhibitory profile against AChE (0.048 ± 0.007 μM), BChE (0.89 ± 0.018 μM), and MAO-B (0.95 ± 0.12 μM) enzymes. SAR exploration revealed that the truncation of the linker connecting both the aryl binding sites of the semicarbazone scaffold, by one atom, has relatively suppressed the AChE inhibitory potential. Kinetic studies disclosed that the compound 4i reversibly inhibited AChE enzyme in a competitive manner (K

Indexed as

CholinesterasesMonoamine Oxidase InhibitorsAcetylcholinesteraseBenzoatesCholinesterase InhibitorsHydrazonesKineticsMolecular Docking SimulationMonoamine OxidaseStructure-Activity RelationshipTaurine2-(N-cyclohexylamino)ethanesulfonic acidAcetylcholinesteraseBenzoatesCholinesterase InhibitorsCholinesterasesHydrazonesMonoamine OxidaseMonoamine Oxidase Inhibitorspiperonylic acidTaurineCholinesteraseDual inhibitorsHydrazonesMolecular dockingMonoamine oxidasePiperonylic acid

Identifiers

PMID36355337

DOI10.1007/s11030-022-10564-9

OpenAlexW4308682680

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.