Kandandapani, Salanee and Kabir, Md. Zahirul and Tayyab, Hafsa and Mohamad, Saharuddin and Tayyab, Saad (2023) Molecular recognition between anticancer drug, regorafenib and human serum albumin: interaction revisited. Croatica Chemica Acta, 95 (2). pp. 57-68. ISSN 0011-1643, DOI https://doi.org/10.5562/cca3922.
Full text not available from this repository.Abstract
The wet-lab techniques (fluorimetry and spectrophotometry), along with computational techniques (molecular docking and molecular dynamics (MD) simulation), were applied to re-examine the association of an anticancer drug, regorafenib (REG) with human serum albumin (HSA). The REG-induced protein fluorescence quenching was characterized as static quenching based on a decrement in the KSV (Stern-Volmer constant) with increasing temperature and hyperchromic effect in the absorption spectra. The REG-HSA complex (Ka = 0.63 - 1.17 x 105 M-1) was stabilized by hydrophobic and van der Waals interactions in combination with hydrogen bonds, as revealed by thermodynamic data (& UDelta;rS' = +17.17 J mol-1 K-1 and & UDelta;rH' = -23.00 kJ mol-1), and further supported by molecular docking assessment. Microenvironmental fluctuations around HSA fluorophores and better protein stability against thermal stress were evident due to REG-HSA complexation. Accessibility of both Sudlow's Sites I and II but priority for Site I of the protein for REG was inferred by the competitive ligand displacement and molecular docking assessments. MD simulation results supported the stability of the complex.
| Item Type: | Article |
|---|---|
| Funders: | Universiti Malaya Frontier Research Grant (FRG) 2017 FG025-17AFR |
| Uncontrolled Keywords: | Human serum albumin; Regorafenib; Fluorescence quenching; Ligand-protein interaction |
| Subjects: | Q Science > QD Chemistry |
| Divisions: | Faculty of Science > Institute of Biological Sciences |
| Depositing User: | Ms. Juhaida Abd Rahim |
| Date Deposited: | 08 Nov 2025 11:00 |
| Last Modified: | 08 Nov 2025 11:00 |
| URI: | http://eprints.um.edu.my/id/eprint/49740 |
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