Exploring the interaction between tyrphostin 9 and human serum albumin using biophysical and computational methods

Kandandapani, Salanee and Ridzwan, Nor Farrah Wahidah and Mohamad, Saharuddin and Tayyab, Saad (2020) Exploring the interaction between tyrphostin 9 and human serum albumin using biophysical and computational methods. Journal of Biomolecular Structure and Dynamics, 38 (14). pp. 4134-4142. ISSN 0739-1102, DOI https://doi.org/10.1080/07391102.2019.1673210.

Full text not available from this repository.


Tyrphostin 9 (Tyr 9) is a potent platelet-derived growth factor receptor (PDGFR) inhibitor, which induces apoptosis in various cancer cell types. The binding of Tyr 9 to the major transport protein, human serum albumin (HSA) was investigated using several spectroscopic techniques and molecular docking method. Fluorescence quenching titration results showed progressive decrease in the protein fluorescence with increasing drug concentrations. A decreasing trend of the Stern-Volmer constant, K-sv with increasing temperature characterized the drug-induced quenching as static quenching, thus pointed towards the formation of Tyr 9?HSA complex. The binding constant of Tyr 9?HSA interaction was found to lie within the range 3.48?1.69???10(5) M-?1 at three different temperatures, i.e. 15 ?C, 25 ?C and 35??C, respectively and suggested intermediate binding affinity between Tyr 9 and HSA. The drug?HSA complex seems to be stabilized by hydrophobic forces, van der Waals forces and hydrogen bonds, as suggested from the thermodynamic data as well as molecular docking results. The far-UV and the near-UV CD spectral results showed slight alteration in the secondary and tertiary structures, respectively, of the protein upon Tyr 9 binding. Interaction of Tyr 9 with HSA also produced microenvironmental perturbations around protein fluorophores, as evident from the three-dimensional fluorescence spectral results but increased protein?s thermal stability. Both competitive drug binding results and molecular docking analysis suggested Sudlow?s Site I of HSA as the preferred Tyr 9 binding site. Communicated by Ramaswamy H. Sarma

Item Type: Article
Funders: Universiti Malaya (FG025-17AFR)
Uncontrolled Keywords: Tyrphostin 9; Human serum albumin; Fluorescence quenching; Drug?protein interaction; Molecular docking
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science > Institute of Biological Sciences
Depositing User: Ms Zaharah Ramly
Date Deposited: 06 Mar 2023 03:57
Last Modified: 06 Mar 2023 03:57
URI: http://eprints.um.edu.my/id/eprint/37272

Actions (login required)

View Item View Item