NMR study on the low-affinity interaction of human serum albumin with diclofenac sodium |
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Authors: | Ji Zhu-Sheng Li Cong-Gang Mao Xi-An Liu Mai-Li Hu Ji-Ming |
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Affiliation: | Department of Analysis-Measurement Science, Wuhan University, Wuhan, P R China. |
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Abstract: | 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. |
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