| Autor: |
Oscar H. Martínez-Costa, Laura Rodrigues-Miranda, Sofia M. Clemente, António Jorge Parola, Nuno Basilio, Alejandro K. Samhan-Arias |
| Přispěvatelé: |
DQ - Departamento de Química, LAQV@REQUIMTE |
| Jazyk: |
angličtina |
| Rok vydání: |
2023 |
| Předmět: |
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| Zdroj: |
Molecules; Volume 28; Issue 1; Pages: 123 |
| Popis: |
Authors would like to acknowledge the Biochemistry Department in the Faculty of Medicine at the Universidad Autónoma de Madrid for the equipment and support for some of the required reagent purchases. FCT/MCTES is also acknowledged for supporting the National Portuguese NMR Network (ROTEIRO/0031/2013-PINFRA/22161/2016, co-financed by FEDER through COMPETE 2020, POCI, PORL. We thank José Paulo da Silva for the HRMS-ESI analysis. Publisher Copyright: © 2022 by the authors. Cytochrome b5 reductase (Cb5R) is a flavoprotein that participates in the reduction of multiple biological redox partners. Co-localization of this protein with nitric oxide sources has been observed in neurons. In addition, the generation of superoxide anion radical by Cb5R has been observed. A search for specific inhibitors of Cb5R to understand the role of this protein in these new functions has been initiated. Previous studies have shown the ability of different flavonoids to inhibit Cb5R. Anthocyanins are a subgroup of flavonoids responsible for most red and blue colors found in flowers and fruits. Although usually represented by the flavylium cation form, these species are only stable at rather acidic pH values (pH ≤ 1). At higher pH values, the flavylium cation is involved in a dynamic reaction network comprising different neutral species with the potential ability to inhibit the activities of Cb5R. This study aims to provide insights into the molecular mechanism of interaction between flavonoids and Cb5R using flavylium salts as dynamic inhibitors. The outcome of this study might lead to the design of improved specific enzyme inhibitors in the future. publishersversion published |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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