Affiliations: Department of Chemistry, Nanjing Xiaozhuang University, Nanjing 210017, P. R. China | Center for Instrumental Analysis, China Pharmaceutical University, Nanjing 210009, P. R. China
Note: [] Corresponding author: C. Chen, Department of Chemistry, Nanjing Xiaozhuang University, Nanjing 210017, P. R. China. Tel.: +86 25 86569262; E-mail: yhjiangccy@126.com.
Abstract: 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 7.12×104 l mol−1, 4.66×104 l mol−1, respectively. The standard enthalpy change (ΔH0) and the standard entropy change (ΔS0) 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.
