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Natural Polyprenylated Benzophenones Inhibiting Cysteine and Serine Proteases by Felipe T. Martins; Diego M. Assis; Marcelo H. dos Santos; I. Camps; Márcia P. Veloso; Maria A. Juliano; Lira C. Alves; Antônio C. Doriguetto is a Chemistry article available to read on EtoBox.
What is Natural Polyprenylated Benzophenones Inhibiting Cysteine and Serine Proteases about?
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 0 ,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 AE 0.1 mM) on such peptidase is quite similar to that of the classical inhibitor of serine proteases, chymostatin (2.1 AE 0.1 mM). 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 activit
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- Author
- Felipe T. Martins; Diego M. Assis; Marcelo H. dos Santos; I. Camps; Márcia P. Veloso; Maria A. Juliano; Lira C. Alves; Antônio C. Doriguetto
- Publisher
- Elsevier Science; Elsevier ; Elsevier BV (ISSN 0223-5234)
- Published
- 2009
- Language
- EN
- Field
- Chemistry (Physical Sciences)