Interaction of 5-fluoro-5′-deoxyuridine with human serum albumin under physiological and non-physiological condition: A biophysical investigation

- Binding affinity of 5′dFUrd to HSA was higher at physiological pH (7.4) in compare to non-physiological pH (9.0).
- Interaction of 5′dFUrd to HSA induced prominent conformational changes at physiological pH in compare to non-physiological pH.
- Thermal stability of protein drug complex was higher at physiological pH in comparison to non-physiological pH.
- Site specific probe binding experiment and molecular docking studies suggested that 5′dFUrd was mainly bound to subdomain IIA, Sudlow's site I of HSA.