Spectroscopic analysis of the interaction between 1-Adamantanecarboxylic acid and bovine serum albumin

Objective To study on the interaction between bovine serum albumin(BSA) and 1-Adamantanecarboxylic acid(Ad). Methods The interaction of Ad and BSA was observed with fluorescence,UV/vis and Circular Dichroism(CD) Spectroscopy techniques.Results The binding constants KA of Ad with BSA at 291 K and 301 K were(7.83±0.01)×104 L·mol-1 and(1.59±0.01)×104 L·mol-1 respectively.There was only one binding site on BSA for Ad binding.The results indicated that hydrogen bond and Van Der Waals interaction were involved in the binding process.The average binding distance between the donor(BSA) and the acceptor Ad was obtained(r=3.12 nm).The α-helical structure of BSA reduced from 22.4% to 19.6%,and the β-sheet content increased from 30.2% to 43.6%.Conclusion The experimental results showed that Ad caused the fluorescence quenching of BSA through a static quenching procedure and the binding changes its secondary structure.