Natural polyprenylated benzophenones inhibiting cysteine and serine proteases

Show simple item record Martins, Felipe T. Assis, Diego M. Santos, Marcelo H. dos Camps, I. Veloso, Marcia P. Juliano, Maria A. [UNIFESP] Alves, Lira C. Doriguetto, Antonio C. 2016-01-24T13:52:19Z 2016-01-24T13:52:19Z 2009-03-01
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.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.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


File Size Format View

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record




My Account