Investigation of the interaction between amodiaquine and human serum albumin by fluorescence spectroscopy and molecular modeling.
The interaction of amodiaquine (AQ) with human serum albumin (HSA) has been studied by fluorescence spectroscopy. Based on the sign and magnitude of the enthalpy and entropy changes (ΔH(0) = -43.27 kJ mol(-1) and ΔS(0) = -50.03 J mol(-1) K(-1)), hydrogen bond and van der Waals forces were suggested as the main interacting forces. Moreover, the efficiency of energy transfer and distance between HSA and acceptor AQ was calculated. Finally, the binding of AQ to HSA was modeled by molecular docking and molecular dynamic simulation methods. Excellent agreement was found between the experimental and theoretical results. Both experimental results and modeling methods suggested that AQ binds mainly to the sub-domain IIA of HSA.
Department of Chemistry, Shiraz University, Department of Chemistry, Adabiat Four-way, Shiraz, Fars 71454, Iran.
Fayezeh
F
Samari
Mojtaba
M
Shamsipur
Bahram
B
Hemmateenejad
Taghi
T
Khayamian
Sajjad
S
Gharaghani
D000655:Amodiaquine / Q000378:metabolism* / Q000494:pharmacology; D000962:Antimalarials / Q000378:metabolism* / Q000494:pharmacology; D004735:Energy Transfer; D006801:Humans; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D011485:Protein Binding; D011487:Protein Conformation / Q000187:drug effects; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics
D000962:Antimalarials; D012709:Serum Albumin; D000655:Amodiaquine