Influence of Rutin, Sinapic Acid, and Naringenin on Binding of Tyrosine Kinase Inhibitor Erlotinib to Bovine Serum Albumin Using Analytical Techniques Along with Computational Approach
Flavonoid-containing food supplements are widely used as antioxidants, and the continuous use of these supplements with other drugs can lead to clinically significant interactions between these and other drugs. The medications in systemic circulation are mainly transported by serum albumin, a major...
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MDPI AG
2022-03-01
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| author | Tanveer A. Wani Ahmed H. Bakheit Seema Zargar Arwa Ishaq A. Khayyat Abdulrahman A. Al-Majed |
| author_facet | Tanveer A. Wani Ahmed H. Bakheit Seema Zargar Arwa Ishaq A. Khayyat Abdulrahman A. Al-Majed |
| author_sort | Tanveer A. Wani |
| collection | DOAJ |
| description | Flavonoid-containing food supplements are widely used as antioxidants, and the continuous use of these supplements with other drugs can lead to clinically significant interactions between these and other drugs. The medications in systemic circulation are mainly transported by serum albumin, a major transport protein. This study evaluated the interactions of rutin (RUT), naringenin (NAR), and sinapic acid (SIN) with the most abundant transport protein, bovine serum albumin (BSA), and the anticancer drug, the tyrosine kinase inhibitor Erlotinib (ETB), using various analytical methods. Interaction between multiple types of ligands with the transport proteins and competition between themselves can lead to the bound ETB’s displacement from the BSA-binding site, leading to elevated ETB concentrations in the systemic circulation. These elevated drug fractions can lead to adverse events and lower tolerance, and increased resistance to the therapeutic regimen of ETB. The experimental and computational methods, including molecular-docking studies, were used to understand the molecular interactions. The results suggested that the complexes formed were utterly different in the binary and the ternary system. Furthermore, comparing the ternary systems amongst themselves, the spectra differed from each other. They thus inferred that complexes formed between BSA-ETB in the presence of each RUT, NAR, and SIN separately were also different, with the highest value of the reduction in the binding energy in RUT, followed by SIN and then NAR. Thus, we conclude that a competitive binding between the ETB and these flavonoids might influence the ETB pharmacokinetics in cancer patients by increasing ETB tolerance or resistance. |
| first_indexed | 2024-03-09T12:06:51Z |
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| id | doaj.art-9bba642d3e524bc29fa5fb7fe3a771a3 |
| institution | Directory Open Access Journal |
| issn | 2076-3417 |
| language | English |
| last_indexed | 2024-03-09T12:06:51Z |
| publishDate | 2022-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Applied Sciences |
| spelling | doaj.art-9bba642d3e524bc29fa5fb7fe3a771a32023-11-30T22:57:38ZengMDPI AGApplied Sciences2076-34172022-03-01127357510.3390/app12073575Influence of Rutin, Sinapic Acid, and Naringenin on Binding of Tyrosine Kinase Inhibitor Erlotinib to Bovine Serum Albumin Using Analytical Techniques Along with Computational ApproachTanveer A. Wani0Ahmed H. Bakheit1Seema Zargar2Arwa Ishaq A. Khayyat3Abdulrahman A. Al-Majed4Department of Pharmaceutical Chemistry, College of Pharmacy, King Saud University, P.O. Box 2457, Riyadh 11451, Saudi ArabiaDepartment of Pharmaceutical Chemistry, College of Pharmacy, King Saud University, P.O. Box 2457, Riyadh 11451, Saudi ArabiaDepartment of Biochemistry, College of Science, King Saud University, P.O. Box 22452, Riyadh 11451, Saudi ArabiaDepartment of Biochemistry, College of Science, King Saud University, P.O. Box 22452, Riyadh 11451, Saudi ArabiaDepartment of Pharmaceutical Chemistry, College of Pharmacy, King Saud University, P.O. Box 2457, Riyadh 11451, Saudi ArabiaFlavonoid-containing food supplements are widely used as antioxidants, and the continuous use of these supplements with other drugs can lead to clinically significant interactions between these and other drugs. The medications in systemic circulation are mainly transported by serum albumin, a major transport protein. This study evaluated the interactions of rutin (RUT), naringenin (NAR), and sinapic acid (SIN) with the most abundant transport protein, bovine serum albumin (BSA), and the anticancer drug, the tyrosine kinase inhibitor Erlotinib (ETB), using various analytical methods. Interaction between multiple types of ligands with the transport proteins and competition between themselves can lead to the bound ETB’s displacement from the BSA-binding site, leading to elevated ETB concentrations in the systemic circulation. These elevated drug fractions can lead to adverse events and lower tolerance, and increased resistance to the therapeutic regimen of ETB. The experimental and computational methods, including molecular-docking studies, were used to understand the molecular interactions. The results suggested that the complexes formed were utterly different in the binary and the ternary system. Furthermore, comparing the ternary systems amongst themselves, the spectra differed from each other. They thus inferred that complexes formed between BSA-ETB in the presence of each RUT, NAR, and SIN separately were also different, with the highest value of the reduction in the binding energy in RUT, followed by SIN and then NAR. Thus, we conclude that a competitive binding between the ETB and these flavonoids might influence the ETB pharmacokinetics in cancer patients by increasing ETB tolerance or resistance.https://www.mdpi.com/2076-3417/12/7/3575Erlotinibbovine serum albuminfluorescence quenchingbinding interactionrutinnaringenin |
| spellingShingle | Tanveer A. Wani Ahmed H. Bakheit Seema Zargar Arwa Ishaq A. Khayyat Abdulrahman A. Al-Majed Influence of Rutin, Sinapic Acid, and Naringenin on Binding of Tyrosine Kinase Inhibitor Erlotinib to Bovine Serum Albumin Using Analytical Techniques Along with Computational Approach Applied Sciences Erlotinib bovine serum albumin fluorescence quenching binding interaction rutin naringenin |
| title | Influence of Rutin, Sinapic Acid, and Naringenin on Binding of Tyrosine Kinase Inhibitor Erlotinib to Bovine Serum Albumin Using Analytical Techniques Along with Computational Approach |
| title_full | Influence of Rutin, Sinapic Acid, and Naringenin on Binding of Tyrosine Kinase Inhibitor Erlotinib to Bovine Serum Albumin Using Analytical Techniques Along with Computational Approach |
| title_fullStr | Influence of Rutin, Sinapic Acid, and Naringenin on Binding of Tyrosine Kinase Inhibitor Erlotinib to Bovine Serum Albumin Using Analytical Techniques Along with Computational Approach |
| title_full_unstemmed | Influence of Rutin, Sinapic Acid, and Naringenin on Binding of Tyrosine Kinase Inhibitor Erlotinib to Bovine Serum Albumin Using Analytical Techniques Along with Computational Approach |
| title_short | Influence of Rutin, Sinapic Acid, and Naringenin on Binding of Tyrosine Kinase Inhibitor Erlotinib to Bovine Serum Albumin Using Analytical Techniques Along with Computational Approach |
| title_sort | influence of rutin sinapic acid and naringenin on binding of tyrosine kinase inhibitor erlotinib to bovine serum albumin using analytical techniques along with computational approach |
| topic | Erlotinib bovine serum albumin fluorescence quenching binding interaction rutin naringenin |
| url | https://www.mdpi.com/2076-3417/12/7/3575 |
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