title: Interaction between a cationic porphyrin and bovine serum albumin studied by surface plasmon resonance, fluorescence spectroscopy and cyclic voltammetry.
abstract: The interaction between a cationic porphyrin and bovine serum albumin (BSA) was studied by using surface plasmon resonance (SPR) spectroscopy, which was combined with fluorescence quenching method and cyclic voltammetric method to confirm the binding kinetic results. In this paper, the SPR method used to study the drug-protein interaction was described in detail. The association rate constant, dissociation rate constant and the equilibrium association constant of porphyrin binding to BSA obtained from this method were 1067 ± 18.23 M(-1) s(-1), 0.01644 ± 0.00012 s(-1), and 6.49 × 10(4) M(-1), respectively. The equilibrium association constants obtained from the fluorescence quenching method and the cyclic voltammetric method were 1.102 × 10(5) M(-1) and 1.21 × 10(5) M(-1), respectively.
authors: State Key Laboratory of Virology & College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, P. R. China.
authors: Chang-Qing
authors: CQ
authors: Xiao
authors: Feng-Lei
authors: FL
authors: Jiang
authors: Bo
authors: B
authors: Zhou
authors: Ran
authors: R
authors: Li
authors: Yi
authors: Y
authors: Liu
mesh_terms: D000818:Animals; D002412:Cations / Q000737:chemistry; D002417:Cattle; D055664:Electrochemical Techniques; D007700:Kinetics; D011166:Porphyrins / Q000737:chemistry*; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D020349:Surface Plasmon Resonance
chemical_list: D002412:Cations; D011166:Porphyrins; D012710:Serum Albumin, Bovine