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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Eleocarpanthraquinone, a novel anthraquinone from Rhamnidium elaeocarpum (Rhamnaceae)

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Autor(es):
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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]
Número total de Autores: 13
Afiliação do(s) autor(es):
[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
Número total de Afiliações: 3
Tipo de documento: Artigo Científico
Fonte: Tetrahedron Letters; v. 61, n. 45 NOV 5 2020.
Citações Web of Science: 0
Resumo

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)

Processo FAPESP: 16/25112-4 - Avaliação de moduladores da atividade de proteases envolvidas em processos patológicos
Beneficiário:Wagner Alves de Souza Júdice
Linha de fomento: Auxílio à Pesquisa - Regular