| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 599516 | Colloids and Surfaces B: Biointerfaces | 2014 | 9 Pages |
Abstract
- Binding affinity of 5â²dFUrd to HSA was higher at physiological pH (7.4) in compare to non-physiological pH (9.0).
- Interaction of 5â²dFUrd 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 5â²dFUrd was mainly bound to subdomain IIA, Sudlow's site I of HSA.
Keywords
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Colloid and Surface Chemistry
Authors
Mohd Ishtikhar, Gulam Rabbani, Rizwan Hasan Khan,