Natural polyprenylated benzophenones inhibiting cysteine and serine proteases

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dc.contributor.author Martins, Felipe T.
dc.contributor.author Assis, Diego M.
dc.contributor.author Santos, Marcelo H. dos
dc.contributor.author Camps, I.
dc.contributor.author Veloso, Marcia P.
dc.contributor.author Juliano, Maria A. [UNIFESP]
dc.contributor.author Alves, Lira C.
dc.contributor.author Doriguetto, Antonio C.
dc.date.accessioned 2016-01-24T13:52:19Z
dc.date.available 2016-01-24T13:52:19Z
dc.date.issued 2009-03-01
dc.identifier http://dx.doi.org/10.1016/j.ejmech.2008.09.018
dc.identifier.citation European Journal of Medicinal Chemistry. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 44, n. 3, p. 1230-1239, 2009.
dc.identifier.issn 0223-5234
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/31355
dc.description.abstract We 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.sponsorship Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorship Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorship Fundação de Amparo à Pesquisa do Estado de Minas Gerais (FAPEMIG)
dc.description.sponsorship FINEP (Financiadora de Estudos e Projetos)
dc.format.extent 1230-1239
dc.language.iso eng
dc.publisher Elsevier B.V.
dc.relation.ispartof European Journal of Medicinal Chemistry
dc.rights Acesso restrito
dc.subject Benzophenones en
dc.subject Proteases en
dc.subject Guttiferone A en
dc.subject Cathepsin G en
dc.subject SAR en
dc.subject Flexible docking en
dc.title Natural polyprenylated benzophenones inhibiting cysteine and serine proteases en
dc.type Artigo
dc.rights.license http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institution Univ Fed Alfenas
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.description.affiliation Univ Fed Alfenas, Dept Exact Sci, BR-37130000 Alfenas, MG, Brazil
dc.description.affiliation Universidade Federal de São Paulo, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.sponsorshipID FAPEMIG: EDT-3310/06
dc.description.sponsorshipID FINEP (Financiadora de Estudos e Projetos): 1110/06
dc.identifier.doi 10.1016/j.ejmech.2008.09.018
dc.description.source Web of Science
dc.identifier.wos WOS:000264558600035



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