Computational studies on the structural variations of MAO-A and MAO-B inhibitors - An in silico docking approach-Supplementary data

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dc.contributor.authorP Nambiar, Meghaen_US
dc.contributor.authorJayadevan, Sarayuen_US
dc.contributor.authorBabu, BKen_US
dc.contributor.authorBiju, ARen_US
dc.date.accessioned2023-08-09T06:01:40Z
dc.date.available2023-08-09T06:01:40Z
dc.date.issued2022-03
dc.description.abstractThe neurological disorder is a concerning problem in the present social scenario. The malfunction of the monoamine oxidase (MAO) enzyme is the responsible factor behind this disorder because this enzyme regulates the metabolism of monoamine neurotransmitters. This work aimed to design and propose the best MAO inhibitors through extensive computational analysis so that the favourable drug-like molecules could be identified for future synthesis. The drugs selected in this study were three MAO-A inhibitors namely Moclobemide, Tolxatone and Brofaromine and two MAO-B inhibitors namely Selegiline and Rasagiline. By substituting hydrophilic and hydrophobic groups at the specified positions, structural variations were designed for each drug. The designed variations and their parent drugs were optimized (basis set is B3LYP/6-311G(d, p)) and the optimized structures were docked to the target using PyRx software. The binding energy of each variation was compared to that of parent drug. The drug-likeness, physicochemical properties (solubility, polarity, flexibility, gastrointestinal absorption, saturation etc.) and toxicity of the lower binding energy variations were analysed using the swissADME, Osiris property explorer and ProTox-II servers. The interacting residues of the enzymes were obtained from the LigPlot+ program. The safe and low binding energy variations with favourable drug properties are suggested for further drug researchen_US
dc.identifier.affiliationsDepartment of Chemistry, Sir Syed College, Taliparamba-670 141, Kerala, Indiaen_US
dc.identifier.affiliationsDepartment of Engineering Chemistry, Andhra University College of Engineering (A), Visakhapatnam-530 003, Andhra Pradesh, Indiaen_US
dc.identifier.citationP Nambiar Megha, Jayadevan Sarayu, Babu BK, Biju AR. Computational studies on the structural variations of MAO-A and MAO-B inhibitors - An in silico docking approach-Supplementary data. Indian Journal of Biochemistry & Biophysics. 2022 Mar; 59(3): 276-295en_US
dc.identifier.issn0019-5189
dc.identifier.issn0975-1009
dc.identifier.placeIndiaen_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/221499
dc.languageenen_US
dc.publisherCSIR-NIScPRen_US
dc.relation.issuenumber3en_US
dc.relation.volume59en_US
dc.source.urihttps://doi.org/10.56042/ijbb.v59i3.42431en_US
dc.subjectBinding energyen_US
dc.subjectDrug-likenessen_US
dc.subjectMonoamine oxidaseen_US
dc.subjectNeurotransmittersen_US
dc.subjectOptimizationen_US
dc.titleComputational studies on the structural variations of MAO-A and MAO-B inhibitors - An in silico docking approach-Supplementary dataen_US
dc.typeJournal Articleen_US
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