Comparative Studies on the Interaction of Human and Bovine Serum Albumins with Vitamin C

Abstract

The interactions of human and bovine serum albumins (HSA and BSA) with various drugs using spectroscopic techniques have received great attention now a days due to their significant effect in the biomedical field. UV absorption and fluorescence spectroscopy are the most likable due to its high sensitivity and simplicity. The interaction of HSA and BSA with vitamin C was investigated. Results showed that the absorption and fluorescence intensities increased as the vitamin C concentration increases. The calculated binding constant (k ~104 M-1) showed a week binding of vitamin C with both serum albumins. The analysis of fluorescence quenching for HSA/BSA-vitamin C interaction (kq ~ 1011 L mol-1 s-1) reveals the dynamic quenching process and clearly confirms the existence of static mechanism of fluorescence quenching.