Study of BSA -Caffeine interaction by UV –Visible spectroscopy

In this research, we have used UV –Visible spectroscopy to study of the interaction of caffeine (Caf) with bovine serum albumin (BSA) in aqueous solution (pH ۷.۴) at ۳۱۰ K. The results of UV –visible spectroscopy showed that Caf bonded to BSA with an overall binding constant of KBSA-Caf = ۱.۸۵ (±۰.۱۱)×۱۰۳ M−۱ suggesting moderate binding between the Caf and BSA. This binding affinity, which describes the strength of the interaction between drug and protein, is crucial for assessing the pharmacokinetic properties that influence clinical studies

کلیدواژه ها:

Caffeine ، Bovine serum albumin ، Binding Constant ، UV –Visible spectroscopy