Natural polyprenylated benzophenones inhibiting cysteine and serine proteases

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dc.contributor.authorMartins, Felipe T.
dc.contributor.authorAssis, Diego M.
dc.contributor.authorSantos, Marcelo H. dos
dc.contributor.authorCamps, I.
dc.contributor.authorVeloso, Marcia P.
dc.contributor.authorJuliano, Maria A. [UNIFESP]
dc.contributor.authorAlves, Lira C.
dc.contributor.authorDoriguetto, Antonio C.
dc.contributor.institutionUniv Fed Alfenas
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T13:52:19Z
dc.date.available2016-01-24T13:52:19Z
dc.date.issued2009-03-01
dc.description.abstractWe have investigated the in vitro inhibition of papain, trypsin, and cathepsins B and G by five benzophenone-type compounds, three natural ones isolated from Garcinia brasiliensis and two synthetic derivatives. the activities of pentaprenylated trihydroxy-substituted benzophenone guttiferone A (1) on all assayed enzymes were approximately 2-69 folds higher than that manifested by mono-hydroxylated tetraprenylated and triprenylated compounds epiclusianone (2) and garciniaphenone (3), respectively, the other natural benzophenones that also inhibited significantly the four enzymes. Differently, the synthetic derivatives 2,2',4-trihydroxybenzophenone (4) and diphenylmethanone (5) have inhibited weakly the studied proteases. Furthermore, compound 1 has bonded preferentially to cathepsin G, once its IC(50) value (2.7 +/- 0.1 mu M) on such peptidase is quite similar to that of the classical inhibitor of serine proteases, chymostatin (2.1 +/- 0.1 mu M). Interesting structure-activity relationships (SARs) were confirmed by flexible docking simulations, likewise the potential usefulness of natural compound 1 as antitumoral drug is strengthened by our results concerning the antiproteolytic activity. (C) 2008 Elsevier Masson SAS. All rights reserved.en
dc.description.affiliationUniv Fed Alfenas, Dept Exact Sci, BR-37130000 Alfenas, MG, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de Minas Gerais (FAPEMIG)
dc.description.sponsorshipFINEP (Financiadora de Estudos e Projetos)
dc.description.sponsorshipIDFAPEMIG: EDT-3310/06
dc.description.sponsorshipIDFINEP (Financiadora de Estudos e Projetos): 1110/06
dc.format.extent1230-1239
dc.identifierhttp://dx.doi.org/10.1016/j.ejmech.2008.09.018
dc.identifier.citationEuropean Journal of Medicinal Chemistry. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 44, n. 3, p. 1230-1239, 2009.
dc.identifier.doi10.1016/j.ejmech.2008.09.018
dc.identifier.issn0223-5234
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/31355
dc.identifier.wosWOS:000264558600035
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofEuropean Journal of Medicinal Chemistry
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectBenzophenonesen
dc.subjectProteasesen
dc.subjectGuttiferone Aen
dc.subjectCathepsin Gen
dc.subjectSARen
dc.subjectFlexible dockingen
dc.titleNatural polyprenylated benzophenones inhibiting cysteine and serine proteasesen
dc.typeinfo:eu-repo/semantics/article
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