Interaction of rhein with human serum albumin investigation by optical spectroscopic technique and modeling studies.
The binding of rhein with human serum albumin (HSA) has been studied in detail by spectroscopic method including circular dichroism (CD), Fourier transformation infrared spectra (FT-IR), fluorescence spectra. The binding parameters for the reaction have been calculated according to Scatchard equation at different temperatures. The plots indicated that the binding of HSA to rhein at 303, 310 and 318 K is characterized by one binding site with the affinity constant K at (4.93+/-0.16)x10(5), (4.02+/-0.16)x10(5) and (2.69+/-0.16)x10(5) M-1, respectively. The secondary structure compositions of free HSA and its rhein complexes were estimated by the FT-IR spectra. FT-IR and curve-fitted results of amide I band are in good agreement with the analyses of CD spectra. Molecular Modeling method was used to calculate the interaction modes between the drug and HSA.
Li
Ying
Y
Department of chemistry, LanZhou University, LanZhou 730000, China.
Yao
Xiaojun
X
Jin
Jing
J
Chen
Xingguo
X
Hu
Zhide
Z
D000880:Anthraquinones / Q000737:chemistry*; D001665:Binding Sites; D001667:Binding, Competitive; D002942:Circular Dichroism; D006801:Humans; D008958:Models, Molecular; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared; D013816:Thermodynamics
D000880:Anthraquinones; D012709:Serum Albumin; C020491:rhein