Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/31355
Title: Natural polyprenylated benzophenones inhibiting cysteine and serine proteases
Authors: 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.
Univ Fed Alfenas
Universidade Federal de São Paulo (UNIFESP)
Keywords: Benzophenones
Proteases
Guttiferone A
Cathepsin G
SAR
Flexible docking
Issue Date: 1-Mar-2009
Publisher: Elsevier B.V.
Citation: European Journal of Medicinal Chemistry. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 44, n. 3, p. 1230-1239, 2009.
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.
URI: http://repositorio.unifesp.br/handle/11600/31355
ISSN: 0223-5234
Other Identifiers: http://dx.doi.org/10.1016/j.ejmech.2008.09.018
Appears in Collections:Em verificação - Geral

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