Interaction of aspirin and vitamin C with bovine serum albumin

Vitamin C (L-ascorbic acid) has a major biological role as a natural antioxidant. Aspirin belongs to the nonsteroidal anti-inflammatory drugs and functions as an antioxidant via its ability to scavenge-OH radicals. Bovine serum albumin (BSA) is the major soluble protein constituent of the circulatory system and has many physiological functions including transport of a variety of compounds. In this report, the competitive binding of vitamin C and aspirin to bovine serum albumin has been studied using constant protein concentration and various drug concentrations at pH 7.2. FTIR and UV–Vis spectroscopic methods were used to analyze vitamin C and aspirin binding modes, the binding constants and the effects of drug complexation on BSA stability and conformation. Spectroscopic evidence showed that vitamin C and aspirin bind BSA via hydrophilic interactions (polypeptide and amine polar groups) with overall binding constants of Kvitamin C-BSA = 1.57 × 104 M−1 and Kaspirin-BSA = 1.15 × 104 M−1; assuming that there is one drug molecule per protein. The BSA secondary structure was altered with major decrease of α-helix from 64% (free protein) to 57% (BSA-vitamin C) and 54% (BSA-aspirin) and β-sheet from 15% (free protein) to 6–7% upon drug complexation, inducing a partial protein destabilization.

► The binding constant of vitamin C-BSA was measured higher than aspirin-BSA. ► At low drugs concentration, no major protein conformational changes occur. ► At high drugs contents, significant decrease of secondary structures was observed. ► A partial protein destabilization was occurred at high drug concentrations. ► BSA can be considered as a good carrier for vitamin C and aspirin in vitro.