Fluorescence spectrometric study on the interaction of tamibarotene with bovine serum albumin.
The interaction between tamibarotene and bovine serum albumin (BSA) was studied using fluorescence quenching technique and ultraviolet-visible spectrophotometry. The results of experiments showed that tamibarotene could strongly quench the intrinsic fluorescence of BSA by a dynamic quenching mechanism. The apparent binding constant, number of binding site and corresponding thermodynamic parameters at different temperatures were calculated respectively, and the main interaction force between tamibarotene and BSA was proved to be hydrophobic force. Synchronous fluorescence spectra showed that tamibarotene changed the molecular conformation of BSA. When BSA concentration was 1.00 × 10⁻⁶mol L⁻¹, the quenched fluorescence ΔF had a good linear relationship with the concentration of tamibarotene in the range 1.00 × 10⁻⁶ to 12.00 × 10⁻⁶ mol L⁻¹ with the detection limit of 6.52 × 10⁻⁷  mol L⁻¹.
Ministry of Education Key Laboratory of Analysis and Detection for Food Safety, Fujian Provincial Key Laboratory of Analysis and Detection for Food Safety, Department of Chemistry, Fuzhou University, Fuzhou, Fujian 350002, China.
Huazhen
H
Ye
Bin
B
Qiu
Zhenyu
Z
Lin
Guonan
G
Chen
D000818:Animals; D001565:Benzoates / Q000737:chemistry*; D002417:Cattle; D007700:Kinetics; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013056:Spectrophotometry, Ultraviolet / Q000379:methods*; D013764:Tetrahydronaphthalenes / Q000737:chemistry*
D001565:Benzoates; D013764:Tetrahydronaphthalenes; C061133:tamibarotene; D012710:Serum Albumin, Bovine