NMR study on the low-affinity interaction of human serum albumin with diclofenac sodium.
The low-affinity interaction between human serum albumin (HSA) and Diclofenac sodium (DCF) was studied using NMR techniques. Both 13C-NMR chemical shift and linewidth show that the dichlorophenyl ring in DCF molecule plays a primary role in its interaction with HSA. Langmuir adsorption isotherm was applied to evaluate the association constant K and the number of binding sites n of the drug/HSA complex through (1)H-NMR spin-lattice relaxation measurement. The results indicate that Langmuir isotherm can perfectly explain the capacity of low-affinity binding of proteins for the ligands.
Ji
Zhu-Sheng
ZS
Department of Analysis-Measurement Science, Wuhan University, Wuhan, P R China.
Li
Cong-Gang
CG
Mao
Xi-An
XA
Liu
Mai-Li
ML
Hu
Ji-Ming
JM
D001665:Binding Sites / Q000502:physiology; D004008:Diclofenac / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism
D012709:Serum Albumin; D004008:Diclofenac