Interaction of pyrrolizine derivatives with bovine serum albumin by fluorescence and UV-Vis spectroscopy.
The interaction between pyrrolizine derivatives (PD) and bovine serum albumin (BSA) under imitated physiological conditions was analyzed by fluorescence and ultraviolet spectra. The experiments were conducted at three different temperatures (302, 306 and 310 K) and the results showed that PD caused the fluorescence quenching of BSA through a combined quenching procedure. The binding constant (K(a)), binding-site number (n) between PD and BSA at different temperatures were obtained. According to Förster non-radiation energy transfer theory, the binding distance (r) between BSA and PD was calculated. The corresponding thermodynamic parameters (ΔG, ΔH, and ΔS) were also obtained. The comparison of binding potency of PD and BSA suggested that the substituent on the benzene ring could enhance the binding affinity of PD and BSA. Finally, we investigated the possible sub-domain on BSA where bind PD by displacement experiments.
Department of Physics, School of Physics and Information Engineering, Fuzhou University, Fuzhou 350108, China.
Jun
J
Zhang
Daxing
D
Xiong
Lingnan
L
Chen
Qilong
Q
Kang
Birong
B
Zeng
D000042:Absorption; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004735:Energy Transfer; D007700:Kinetics; D008024:Ligands; D011485:Protein Binding; D011763:Pyrrolizidine Alkaloids / Q000737:chemistry / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature
D008024:Ligands; D011763:Pyrrolizidine Alkaloids; D012710:Serum Albumin, Bovine