| BINDING OF WARFARIN SODIUM TO BOVINE SERUM ALBUMIN IN PRESENCE OF CAFFEINE: A FLUORESCENCE STUDY |
| Paper ID : 1015-YRC2022 |
| Authors |
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zeinab mohamed anwer1, gasser mohamed khairy1, nada ali salman *2, hend mohamed mostafa3 1suez canal university 2Sinai university 3al-arish university |
| Abstract |
| Studying the interaction of therapeutic molecules with serum albumin is important to understand their biopharmaceutics, pharmacokinetics and toxicity as well as their binding with protein may affected by the presence of any endogenous or exogenous compounds. Hence, The biomolecular interaction of an anticoagulant drug ,warfarin sodium (WS) with bovine serum albumin(BSA) in presence of caffeine(CAF) under physiological condition using tris-HCl buffer solution, pH = 7.4 has been investigated using fluorescence spectroscopic technique. Data collected from fluorescence measurements were analyzed through modified stern volumer equation in order to calculate the binding constant values at room temperature for BSA-Warfarin sodium as binary system and BSA-Caffeine-Warfarin sodium as ternary system . The data reveals that the binding constants values for binary system and ternary system are 1.39×104 mol-1L and 2.9×102 mol-1l respectively at 298 which means that the binding affinity of warfarin sodium to bovine serum albumin decreases in the presence of caffeine. |
| Keywords |
| Bovine Serum Albumin, Caffeine, Fluorescence Spectroscopy. |
| Status: Conditional Accept (Oral Presentation) |
