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New bi-phosphonate derivative: Synthesis, characterization, antioxidant activity in vitro and via cyclic voltammetry mode and evaluation of its inhibition of SARS-CoV-2 main protease

In this study, we have synthesized a new molecule labeled HBPA. Its molecular structure was determined by spectroscopic methods such as: FT-IR, NMR ((1)H, (13)C and (31)P); our compound is subjected to two antioxidant activities assays: DPPH scavenging and ferric reducing antioxidant power (FRAP); i...

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Autores principales: Houas, Noudjoud, Kitouni, Siham, Chafai, Nadjib, Ghedjati, Samira, Djenane, Meriem, Tounsi, Assia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier B.V. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10014130/
https://www.ncbi.nlm.nih.gov/pubmed/36942303
http://dx.doi.org/10.1016/j.molstruc.2023.135356
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author Houas, Noudjoud
Kitouni, Siham
Chafai, Nadjib
Ghedjati, Samira
Djenane, Meriem
Tounsi, Assia
author_facet Houas, Noudjoud
Kitouni, Siham
Chafai, Nadjib
Ghedjati, Samira
Djenane, Meriem
Tounsi, Assia
author_sort Houas, Noudjoud
collection PubMed
description In this study, we have synthesized a new molecule labeled HBPA. Its molecular structure was determined by spectroscopic methods such as: FT-IR, NMR ((1)H, (13)C and (31)P); our compound is subjected to two antioxidant activities assays: DPPH scavenging and ferric reducing antioxidant power (FRAP); in the results, HBPA was expanded remarkable inhibition when compared especially to standard BHT with values of 14.936±0.808 and 7.1486±0.0645 μg/ml, respectively; in addition to the scavenging test of superoxide anion integrated in electrochemical process, it elucidated a strongly stable interaction towards the radical by evaluating the thermodynamic descriptors (Gibbs free energy ΔG° and the binding constant K(b)). Besides, the electrochemical behavior of HBPA was distinguished by an irreversible system and for the electrochemical regime adopted at the surface of the electrode; a diffusion governed by a slow charge transfer was deduced. The molecular docking of HBPA was conducted beside Chloroquine and the obtained results were indicated a significant binding with active sites of the SARS-CoV-2 main protease (M(pro)).
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spelling pubmed-100141302023-03-15 New bi-phosphonate derivative: Synthesis, characterization, antioxidant activity in vitro and via cyclic voltammetry mode and evaluation of its inhibition of SARS-CoV-2 main protease Houas, Noudjoud Kitouni, Siham Chafai, Nadjib Ghedjati, Samira Djenane, Meriem Tounsi, Assia J Mol Struct Article In this study, we have synthesized a new molecule labeled HBPA. Its molecular structure was determined by spectroscopic methods such as: FT-IR, NMR ((1)H, (13)C and (31)P); our compound is subjected to two antioxidant activities assays: DPPH scavenging and ferric reducing antioxidant power (FRAP); in the results, HBPA was expanded remarkable inhibition when compared especially to standard BHT with values of 14.936±0.808 and 7.1486±0.0645 μg/ml, respectively; in addition to the scavenging test of superoxide anion integrated in electrochemical process, it elucidated a strongly stable interaction towards the radical by evaluating the thermodynamic descriptors (Gibbs free energy ΔG° and the binding constant K(b)). Besides, the electrochemical behavior of HBPA was distinguished by an irreversible system and for the electrochemical regime adopted at the surface of the electrode; a diffusion governed by a slow charge transfer was deduced. The molecular docking of HBPA was conducted beside Chloroquine and the obtained results were indicated a significant binding with active sites of the SARS-CoV-2 main protease (M(pro)). Elsevier B.V. 2023-07-15 2023-03-15 /pmc/articles/PMC10014130/ /pubmed/36942303 http://dx.doi.org/10.1016/j.molstruc.2023.135356 Text en © 2023 Elsevier B.V. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Houas, Noudjoud
Kitouni, Siham
Chafai, Nadjib
Ghedjati, Samira
Djenane, Meriem
Tounsi, Assia
New bi-phosphonate derivative: Synthesis, characterization, antioxidant activity in vitro and via cyclic voltammetry mode and evaluation of its inhibition of SARS-CoV-2 main protease
title New bi-phosphonate derivative: Synthesis, characterization, antioxidant activity in vitro and via cyclic voltammetry mode and evaluation of its inhibition of SARS-CoV-2 main protease
title_full New bi-phosphonate derivative: Synthesis, characterization, antioxidant activity in vitro and via cyclic voltammetry mode and evaluation of its inhibition of SARS-CoV-2 main protease
title_fullStr New bi-phosphonate derivative: Synthesis, characterization, antioxidant activity in vitro and via cyclic voltammetry mode and evaluation of its inhibition of SARS-CoV-2 main protease
title_full_unstemmed New bi-phosphonate derivative: Synthesis, characterization, antioxidant activity in vitro and via cyclic voltammetry mode and evaluation of its inhibition of SARS-CoV-2 main protease
title_short New bi-phosphonate derivative: Synthesis, characterization, antioxidant activity in vitro and via cyclic voltammetry mode and evaluation of its inhibition of SARS-CoV-2 main protease
title_sort new bi-phosphonate derivative: synthesis, characterization, antioxidant activity in vitro and via cyclic voltammetry mode and evaluation of its inhibition of sars-cov-2 main protease
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10014130/
https://www.ncbi.nlm.nih.gov/pubmed/36942303
http://dx.doi.org/10.1016/j.molstruc.2023.135356
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