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| Main Authors: | , , , , |
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| Format: | Artículo Open Access |
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Wiley
2024
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| Online Access: | https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/10.1002/bio.4792 |
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| _version_ | 1867004724162592768 |
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| author | Reem N. El Gammal Heba Elmansi Ali A. El‐Emam Fathalla Belal Mohammed E. A. Hammouda |
| author_facet | Reem N. El Gammal Heba Elmansi Ali A. El‐Emam Fathalla Belal Mohammed E. A. Hammouda Reem N. El Gammal Heba Elmansi Ali A. El‐Emam Fathalla Belal Mohammed E. A. Hammouda |
| collection | Wiley Open Access |
| contents | Insights on multi‐spectroscopic approaches for estimating the in vitro binding of favipiravir with adenine nucleotide Reem N. El Gammal Heba Elmansi Ali A. El‐Emam Fathalla Belal Mohammed E. A. Hammouda Luminescence AbstractFavipiravir (FVP) is an oral antiviral drug approved in 2021 for the treatment of COVID‐19. It is a pyrazine derivative that can be integrated into anti‐viral RNA products to inhibit viral replication. While, adenine is a purine nucleobase that is found in deoxyribonucleic acid (DNA) and ribonucleic acid (RNA) to generate genetic information. For the first time, the binding mechanism between FVP and adenine was determined using different techniques, including UV–visible spectrophotometry, spectrofluorimetry, synchronous fluorescence (SF) spectroscopy, Fourier transform infrared (FTIR), fluorescence resonance energy transfer (FRET), and metal ion complexation. The fluorescence spectra indicated that FVP is bound to adenine via Van der Waals forces and hydrogen bonding through a spontaneous binding process (ΔGο < 0). The quenching mechanism was found to be static. Various temperature settings were used to investigate thermodynamic characteristics, such as binding forces, binding constants, and the number of binding sites. The reaction parameters, including the enthalpy change (ΔHο) and entropy change (ΔSο), were calculated using Van't Hoff's equation. The findings demonstrated that the adenine‐FVP binding was endothermic. Furthermore, the results of the experiments revealed that some metal ions (K+, Ca+2, Co+2, Cu+2, and Al+3) might facilitate the binding interaction between FVP and adenine. Slight changes are observed in the FTIR spectra of adenine, indicating the binding interaction between adenine and FVP. This study may be useful in understanding the pharmacokinetic characteristics of FVP and how the drug binds to adenine to prevent any side effects. 10.1002/bio.4792 http://onlinelibrary.wiley.com/termsAndConditions#vor |
| doi_str_mv | 10.1002/bio.4792 |
| format | Artículo Open Access |
| id | wiley_oa_10_1002_bio_4792 |
| institution | Wiley Open Access |
| license_str_mv | http://onlinelibrary.wiley.com/termsAndConditions#vor |
| publishDate | 2024 |
| publisher | Wiley |
| record_format | wiley_oa |
| spellingShingle | Insights on multi‐spectroscopic approaches for estimating the in vitro binding of favipiravir with adenine nucleotide Reem N. El Gammal Heba Elmansi Ali A. El‐Emam Fathalla Belal Mohammed E. A. Hammouda Luminescence Insights on multi‐spectroscopic approaches for estimating the in vitro binding of favipiravir with adenine nucleotide Reem N. El Gammal Heba Elmansi Ali A. El‐Emam Fathalla Belal Mohammed E. A. Hammouda Luminescence AbstractFavipiravir (FVP) is an oral antiviral drug approved in 2021 for the treatment of COVID‐19. It is a pyrazine derivative that can be integrated into anti‐viral RNA products to inhibit viral replication. While, adenine is a purine nucleobase that is found in deoxyribonucleic acid (DNA) and ribonucleic acid (RNA) to generate genetic information. For the first time, the binding mechanism between FVP and adenine was determined using different techniques, including UV–visible spectrophotometry, spectrofluorimetry, synchronous fluorescence (SF) spectroscopy, Fourier transform infrared (FTIR), fluorescence resonance energy transfer (FRET), and metal ion complexation. The fluorescence spectra indicated that FVP is bound to adenine via Van der Waals forces and hydrogen bonding through a spontaneous binding process (ΔGο < 0). The quenching mechanism was found to be static. Various temperature settings were used to investigate thermodynamic characteristics, such as binding forces, binding constants, and the number of binding sites. The reaction parameters, including the enthalpy change (ΔHο) and entropy change (ΔSο), were calculated using Van't Hoff's equation. The findings demonstrated that the adenine‐FVP binding was endothermic. Furthermore, the results of the experiments revealed that some metal ions (K+, Ca+2, Co+2, Cu+2, and Al+3) might facilitate the binding interaction between FVP and adenine. Slight changes are observed in the FTIR spectra of adenine, indicating the binding interaction between adenine and FVP. This study may be useful in understanding the pharmacokinetic characteristics of FVP and how the drug binds to adenine to prevent any side effects. 10.1002/bio.4792 http://onlinelibrary.wiley.com/termsAndConditions#vor |
| title | Insights on multi‐spectroscopic approaches for estimating the in vitro binding of favipiravir with adenine nucleotide |
| topic | Luminescence |
| url | https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/10.1002/bio.4792 |