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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/26090
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dc.contributor.authorDanuello, Amanda-
dc.contributor.authorRomeiro, Nelilma C.-
dc.contributor.authorGiesel, Guilherme M.-
dc.contributor.authorPivatto, Marcos-
dc.contributor.authorViegas, Claudio-
dc.contributor.authorVerli, Hugo-
dc.contributor.authorBarreiro, Eliezer J.-
dc.contributor.authorFraga, Carlos A. M.-
dc.contributor.authorCastro, Newton G.-
dc.contributor.authorBolzani, Vanderlan da Silva-
dc.date.accessioned2014-05-20T14:20:16Z-
dc.date.accessioned2016-10-25T17:41:32Z-
dc.date.available2014-05-20T14:20:16Z-
dc.date.available2016-10-25T17:41:32Z-
dc.date.issued2012-01-01-
dc.identifierhttp://dx.doi.org/10.1590/S0103-50532012000100023-
dc.identifier.citationJournal of The Brazilian Chemical Society. São Paulo: Soc Brasileira Quimica, v. 23, n. 1, p. 163-U505, 2012.-
dc.identifier.issn0103-5053-
dc.identifier.urihttp://hdl.handle.net/11449/26090-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/26090-
dc.description.abstractThe mixture of semi-synthetic derivatives (-)-3-O-acetyl-cassine hydrochloride and (-)-3-O-acetyl-spectaline hydrochloride, prepared from the mixture of natural alkaloids (-)-cassine and (-)-spectaline (4:1) isolated from Senna spectabilis, has been shown to be a potent acetylcholinesterase (AChE) inhibitor, thereby prompting further molecular studies. In this sense, docking and dynamic molecular studies were carried out in this work, aiming to acquire a deeper understanding about all the structural aspects of molecules (-)-3-O-acetyl-cassine and (-)-3-O-acetyl-spectaline hydrochlorides, which differ with respect to their AChE inhibitory potentials. Both molecules establish important interactions with the peripheral anionic site within the catalytic gorge of Torpedo californica AChE. However, only the major compound (-)-3-O-acetyl-cassine hydrochloride significantly interacts with the catalytic triad. Explicit-solvent molecular dynamic simulations were conducted in order to gain better understanding about the hypothetical interactions taking place between the semi-synthetic alkaloid molecules (-)-3-O-acetyl-cassine and (-)-3-O-acetyl-spectaline hydrochlorides and AChE. The data obtained in this study indicated that (-)-3-O-acetyl-cassine hydrochloride is the most potent inhibitor of AChE possibly due to the favorable interactions of this molecule with the target protein, with lower desolvation cost. These results suggested that the size of the side chain has an effect on the inhibitory potential of the evaluated molecules and may represent the starting point for the development of new derivatives of (-)-3-O-acetyl-cassine hydrochloride, with a view to the discovery of new effective AChE inhibitors.en
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ)-
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)-
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
dc.format.extent163-U505-
dc.language.isoeng-
dc.publisherSoc Brasileira Quimica-
dc.sourceWeb of Science-
dc.subjectmolecular dockingen
dc.subjectmolecular dynamicen
dc.subjectpiperidine alkaloidsen
dc.subjectacetylcholinesterase inhibitorsen
dc.titleMolecular Docking and Molecular Dynamic Studies of Semi-Synthetic Piperidine Alkaloids as Acetylcholinesterase Inhibitorsen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniversidade Federal do Rio de Janeiro (UFRJ)-
dc.contributor.institutionUniversidade Federal do Rio Grande do Sul (UFRGS)-
dc.contributor.institutionUniversidade Federal de Alfenas (UNIFAL)-
dc.description.affiliationUniv Estadual Paulista, Dept Quim Organ, Inst Quim, BR-14801970 Araraquara, SP, Brazil-
dc.description.affiliationUniv Fed Rio de Janeiro, Lab Avaliacao & Sintese Subst Bioat LASSBio, Fac Farm, BR-21944910 Rio de Janeiro, RJ, Brazil-
dc.description.affiliationUniversidade Federal do Rio Grande do Sul (UFRGS), Ctr Biotecnol, BR-91500970 Porto Alegre, RS, Brazil-
dc.description.affiliationUniv Fed Alfenas, LFQM, Dept Ciencias Exatas, BR-37130000 Alfenas, MG, Brazil-
dc.description.affiliationUniversidade Federal do Rio Grande do Sul (UFRGS), Fac Farm, BR-90610000 Porto Alegre, RS, Brazil-
dc.description.affiliationUniv Fed Rio de Janeiro, Dept Farmacol Basica & Clin, Inst Ciencias Biomed, BR-21941902 Rio de Janeiro, RJ, Brazil-
dc.description.affiliationUnespUniv Estadual Paulista, Dept Quim Organ, Inst Quim, BR-14801970 Araraquara, SP, Brazil-
dc.description.sponsorshipIdFAPESP: 03/02176-7-
dc.identifier.doi10.1590/S0103-50532012000100023-
dc.identifier.scieloS0103-50532012000100023-
dc.identifier.wosWOS:000300061300024-
dc.rights.accessRightsAcesso aberto-
dc.relation.ispartofJournal of the Brazilian Chemical Society-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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