NMR Study on the Low-Affinity Interaction of Human Serum Albumin with Diclofenac Sodium

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概要

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• The low-affinity interaction between human serum albumin (HSA) and Diclofenac sodium (DCF) was studied using NMR techniques. Both ^<13>C-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 ^1H-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.

• 社団法人日本薬学会の論文
• 2002-08-01

著者

• Li Cong-gang

  Laboratory Of Magnetic Resonance And Atomic And Molecular Physics Wuhan Institute Of Physics And Mat

• JI Zhu-Sheng

  Department of Analysis-Measurement Science, Wuhan University

• MAO Xi-An

  Department of Analysis-Measurement Science, Wuhan University

• LIU Mai-Li

  Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Institute of Physics and Ma

• HU Ji-Ming

  Department of Analysis-Measurement Science, Wuhan University

• Liu Mai-li

  Laboratory Of Magnetic Resonance And Atomic And Molecular Physics Wuhan Institute Of Physics And Mat

• Mao Xi-an

  Department Of Analysis-measurement Science Wuhan University:laboratory Of Magnetic Resonance And Ato

• Hu Ji-ming

  Department Of Analysis-measurement Science Wuhan University

• Ji Zhu-sheng

  Department Of Analysis-measurement Science Wuhan University

関連論文

• NMR Study on the Low-Affinity Interaction of Human Serum Albumin with Diclofenac Sodium

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