Comparison between loureirin A and cochinchinenin C on the interaction with human serum albumin.
The interactions of loureirin A (LA) and cochinchinenin C (CC) with human serum albumin (HSA) under simulated physiological conditions (pH = 7.4) have been studied with fluorescence, UV-vis absorption spectroscopic method and molecular docking technique. The results indicated that there was a synergistic interaction between LA and CC, and the fluorescence quenching of HSA by LA (or CC) was a combined quenching procedure (dynamic and static quenching). At low compound concentrations, the quenching constants KSV of CC was larger than that of LA, which meant the CC efficacy may be better than that of LA. The negative △H and △S values suggested hydrogen bonds and van der Waals forces played the major role in the binding of LA (or CC) to HSA. The efficiency of energy transfer and distance between the compounds and HSA was calculated. Moreover, the results of synchronous and three-dimensional fluorescence demonstrated that the HSA microenvironment was changed in the presence of LA (or CC). Finally, the binding of LA (or CC) to HSA was modeled by molecular docking, which is in good accordance with the experimental studies.
Experimental Center for Life Scinence, Shanghai University, Shanghai, PR China.
Xu
X
Chen
Shanghai Key Lab Bioenergy Crops, School of Life Sciences, Shanghai University, Shanghai, PR China.
Kai
K
Qian
Shanghai Key Lab Bioenergy Crops, School of Life Sciences, Shanghai University, Shanghai, PR China. Electronic address: chenqincc@staff.shu.edu.cn.
Qin
Q
Chen
D001665:Binding Sites; D002599:Chalcone / Q000031:analogs & derivatives* / Q000378:metabolism; D047188:Chalcones / Q000378:metabolism*; D006801:Humans; D062105:Molecular Docking Simulation; D011485:Protein Binding; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*; D013816:Thermodynamics
D047188:Chalcones; D012709:Serum Albumin; C475447:cochinchinenin; C560420:loureirin A; D002599:Chalcone
Cochinchinenin C; Fluorescence quenching; Human serum albumin; Loureirin A; Molecular docking