Multi-spectroscopic analysis and molecular modeling on the interaction of curcumin and its derivatives with human serum albumin: a comparative study.
The comparative study about the interaction between curcumin and its derivatives (demothxycurcumin and bisdeoxycurcumin) with human serum albumin (HSA) has been carried out using multi-spectroscopic analysis and molecular modeling method. The characteristic of fluorescence quenching and the thermodynamic parameters have been studied by state emission fluorescence experiments under different temperatures with an interval of 6 K. Curcumin shows largest quenching constant and bisdeoxycurcumin shows the smallest at the temperature of 298 K. However, the quenching constant of curcumin drops quickly with the increase of temperature. Demothxycurcumin gives the largest quenching efficiency at the temperature of 310 K. An average distance of 6.7 nm for energy transfer has been determined based on förster resonance energy theory (FRET). The site competitive replacement experiments illustrate three compounds mainly binding on site I (Subdomain IIA) of the protein, and show tendency of binding on site II (Subdomain IIIA) with the removing of methoxyl groups. Circular dichroism spectra and Fourier transform infrared spectroscopy (FTIR) have been used to investigate the influence on protein secondary structure. Content of the α-helix increases at low concentrations of the compounds, while unfolding occurs at high concentrations. Docking simulation reveals possible mechanism for different quenching behavior and binding sites preferred by three compounds. The binding modes have effectively supported the conclusion of the experiments.
State Key Laboratory of Virology & Key Laboratory of Analytical Chemistry for Biology and Medicine (Ministry of Education) & College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, PR China.
Yu-Shu
YS
Ge
Institution of Traditional Chinese Medicine of 302 Military Hospital, Beijing 100039, PR China.
Cheng
C
Jin
State Key Laboratory of Virology & Key Laboratory of Analytical Chemistry for Biology and Medicine (Ministry of Education) & College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, PR China.
Zhe
Z
Song
State Key Laboratory of Virology & Key Laboratory of Analytical Chemistry for Biology and Medicine (Ministry of Education) & College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, PR China.
Jia-Qi
JQ
Zhang
State Key Laboratory of Virology & Key Laboratory of Analytical Chemistry for Biology and Medicine (Ministry of Education) & College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, PR China.
Feng-Lei
FL
Jiang
State Key Laboratory of Virology & Key Laboratory of Analytical Chemistry for Biology and Medicine (Ministry of Education) & College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, PR China; College of Chemistry and Materials Science, Hubei Engineering University, Xiaogan 432100, PR China. Electronic address: yiliuchem@whu.edu.cn.
Yi
Y
Liu
D001665:Binding Sites; D002942:Circular Dichroism; D003474:Curcumin / Q000737:chemistry / Q000378:metabolism*; D004735:Energy Transfer; D006801:Humans; D007700:Kinetics; D008958:Models, Molecular; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*; D012996:Solutions; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature
D012709:Serum Albumin; D012996:Solutions; D003474:Curcumin
Binding mode; Curcumin; Human serum albumin; Interaction; Methoxyl groups