This study employs fluorescence spectroscopy to characterize the binding properties of a newly synthesized cardiac agent, V-09, on bovine serum albumin (BSA). This compound shows the highest cardiac activity in the whole series. The binding constants K at 25°C and 37°C are obtained, the values are 7.12×10 4 l mol –1 , 4.66×10 4 l mol –1 , respectively. The standard enthalpy change (Δ H 0 ) and the standard entropy change (Δ S 0 ) are calculated to be –27.13 KJ mol –1 and 1.854 J mol –1 K –1 , which indicated that hydrophobic forces play major role in the interaction between V-09 and BSA. The binding average distance between V-09 and BSA (2.57 nm) is obtained on the basis of the theory of Főrster energy transfer.
Chen, C., Ma, M., Zhang, J., Wang, L., & Xiang, B. (2008). Spectroscopic investigation of the interaction of bovine serum albumin with a novel cardiac agent V-09. Spectroscopy, 22(1), 43–50. https://doi.org/10.1155/2008/450257