Advanced search
Start date
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Eleocarpanthraquinone, a novel anthraquinone from Rhamnidium elaeocarpum (Rhamnaceae)

Full text
Show less -
Kauffmann, Angelica C. [1] ; Oliveira, Rhayssa G. S. P. [1] ; Dourado, Thainara A. [1] ; Soares, Iuri N. [1] ; de Sousa, Paulo T. [1] ; Ribeiro, Tereza A. N. [1] ; Jacinto, Marcos J. [1] ; de Souza, Gabriel L. C. [1] ; Judice, Wagner A. de S. [2] ; Emiliano, Marli de F. C. [2] ; Vianna, Luan dos S. [2] ; de Carvalho, Mario G. [3] ; Silva, Virginia C. P. [1]
Total Authors: 13
[1] Univ Fed Mato Grosso, Dept Quim, BR-78060900 Cuiaba, MT - Brazil
[2] Univ Mogi das Cruzes, Ctr Interdisciplinar Invest Bioquim, BR-08780911 Mogi Das Cruzes, SP - Brazil
[3] Univ Fed Rural Rio de Janeiro, Inst Quim, Dept Quim Organ, BR-23897000 Seropedica, RJ - Brazil
Total Affiliations: 3
Document type: Journal article
Source: Tetrahedron Letters; v. 61, n. 45 NOV 5 2020.
Web of Science Citations: 0

Chemical investigation of the stem bark of Rhamnidium elaeocarpum resulted in the isolation of eleocarpanthraquinone (1), a new anthrone-anthraquinone linked through a spiroketal bridge and the known anthraquinone chrysophanol (2). The structure of (1) was determined by analysis of spectrometry and spectroscopy data, including HRESIMS, 1D, and 2D NMR experiments, and optical rotation data. Eleocarpanthraquinone (1) was able to inhibit the cysteine proteases cathepsins B and L with an inhibitory potential IC50 of 3.69 +/- 0.38 mu M and 1.152 +/- 0.025 mu M, respectively. Both enzymes showed a parabolic competitive inhibition mechanism and an alpha parameter with respective values of 0.00253 and 0.0514, implying a positive cooperativity pathway where the binding of the first molecule potentiates the binding of the second molecule. Conformational analysis was performed using density functional theory at the M06-2X/6-31 + G(d,p) level, indicating that the triply H-bonded conformer was the most stable. (C) 2020 Elsevier Ltd. All rights reserved. (AU)

FAPESP's process: 16/25112-4 - Evaluation of modulators of the activity of proteases involved in pathological processes
Grantee:Wagner Alves de Souza Júdice
Support type: Regular Research Grants