Insights on the in-vitro binding interaction between donepezil and bovine serum albumin
Abstract In this work, the binding mechanism between donepezil (DNP) and bovine serum albumin (BSA) was established using several techniques, including fluorimetry, UV- spectrophotometry, synchronous fluorimetry (SF), fourier transform infrared (FTIR), fluorescence resonance energy transfer (FRET) b...
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| Format: | Article |
| Language: | English |
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BMC
2023-04-01
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| Series: | BMC Chemistry |
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| Online Access: | https://doi.org/10.1186/s13065-023-00944-z |
| _version_ | 1797850221823131648 |
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| author | Reem N. El Gammal Heba Elmansi Ali A. El-Emam Fathalla Belal Perihan A. Elzahhar Ahmed S. F. Belal Mohammed E. A. Hammouda |
| author_facet | Reem N. El Gammal Heba Elmansi Ali A. El-Emam Fathalla Belal Perihan A. Elzahhar Ahmed S. F. Belal Mohammed E. A. Hammouda |
| author_sort | Reem N. El Gammal |
| collection | DOAJ |
| description | Abstract In this work, the binding mechanism between donepezil (DNP) and bovine serum albumin (BSA) was established using several techniques, including fluorimetry, UV- spectrophotometry, synchronous fluorimetry (SF), fourier transform infrared (FTIR), fluorescence resonance energy transfer (FRET) besides molecular docking study. The fluorescence quenching mechanism of DNP-BSA binding was a combined dynamic and static quenching. The thermodynamic parameters, binding forces, binding constant, and the number of binding sites were determined using a different range of temperature settings. Van't Hoff's equation was used to calculate the reaction parameters, including enthalpy change (ΔHο) and entropy change (ΔSο). The results pointed out that the DNP-BSA binding was endothermic. It was shown that the stability of the drug-protein system was predominantly due to the intermolecular hydrophobic forces. Additionally, the site probing method revealed that subdomain IIA (Site I) is where DNP and BSA's binding occurs. This was validated using a molecular docking study with the most stable DNP configuration. This study might help to understand DNP's pharmacokinetics profile and toxicity as well as provides crucial information for its safe use and avoiding its toxicity. |
| first_indexed | 2024-04-09T18:56:55Z |
| format | Article |
| id | doaj.art-3b4260fedd0d40dd8b5adcf79c55ce63 |
| institution | Directory Open Access Journal |
| issn | 2661-801X |
| language | English |
| last_indexed | 2024-04-09T18:56:55Z |
| publishDate | 2023-04-01 |
| publisher | BMC |
| record_format | Article |
| series | BMC Chemistry |
| spelling | doaj.art-3b4260fedd0d40dd8b5adcf79c55ce632023-04-09T11:07:05ZengBMCBMC Chemistry2661-801X2023-04-0117111110.1186/s13065-023-00944-zInsights on the in-vitro binding interaction between donepezil and bovine serum albuminReem N. El Gammal0Heba Elmansi1Ali A. El-Emam2Fathalla Belal3Perihan A. Elzahhar4Ahmed S. F. Belal5Mohammed E. A. Hammouda6Department of Medicinal Chemistry, Faculty of Pharmacy, Mansoura UniversityPharmaceutical Analytical Chemistry Department, Faculty of Pharmacy, Mansoura UniversityDepartment of Medicinal Chemistry, Faculty of Pharmacy, Mansoura UniversityPharmaceutical Analytical Chemistry Department, Faculty of Pharmacy, Mansoura UniversityDepartment of Pharmaceutical Chemistry, Faculty of Pharmacy, Alexandria UniversityDepartment of Pharmaceutical Chemistry, Faculty of Pharmacy, Alexandria UniversityDepartment of Medicinal Chemistry, Faculty of Pharmacy, Mansoura UniversityAbstract In this work, the binding mechanism between donepezil (DNP) and bovine serum albumin (BSA) was established using several techniques, including fluorimetry, UV- spectrophotometry, synchronous fluorimetry (SF), fourier transform infrared (FTIR), fluorescence resonance energy transfer (FRET) besides molecular docking study. The fluorescence quenching mechanism of DNP-BSA binding was a combined dynamic and static quenching. The thermodynamic parameters, binding forces, binding constant, and the number of binding sites were determined using a different range of temperature settings. Van't Hoff's equation was used to calculate the reaction parameters, including enthalpy change (ΔHο) and entropy change (ΔSο). The results pointed out that the DNP-BSA binding was endothermic. It was shown that the stability of the drug-protein system was predominantly due to the intermolecular hydrophobic forces. Additionally, the site probing method revealed that subdomain IIA (Site I) is where DNP and BSA's binding occurs. This was validated using a molecular docking study with the most stable DNP configuration. This study might help to understand DNP's pharmacokinetics profile and toxicity as well as provides crucial information for its safe use and avoiding its toxicity.https://doi.org/10.1186/s13065-023-00944-zDonepezilBovine serum albuminSynchronous fluorimetryFourier transform infraredFluorescence resonance energy transferMolecular docking |
| spellingShingle | Reem N. El Gammal Heba Elmansi Ali A. El-Emam Fathalla Belal Perihan A. Elzahhar Ahmed S. F. Belal Mohammed E. A. Hammouda Insights on the in-vitro binding interaction between donepezil and bovine serum albumin BMC Chemistry Donepezil Bovine serum albumin Synchronous fluorimetry Fourier transform infrared Fluorescence resonance energy transfer Molecular docking |
| title | Insights on the in-vitro binding interaction between donepezil and bovine serum albumin |
| title_full | Insights on the in-vitro binding interaction between donepezil and bovine serum albumin |
| title_fullStr | Insights on the in-vitro binding interaction between donepezil and bovine serum albumin |
| title_full_unstemmed | Insights on the in-vitro binding interaction between donepezil and bovine serum albumin |
| title_short | Insights on the in-vitro binding interaction between donepezil and bovine serum albumin |
| title_sort | insights on the in vitro binding interaction between donepezil and bovine serum albumin |
| topic | Donepezil Bovine serum albumin Synchronous fluorimetry Fourier transform infrared Fluorescence resonance energy transfer Molecular docking |
| url | https://doi.org/10.1186/s13065-023-00944-z |
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