NMR diffusion and relaxation study of drug-protein interaction.
In this work, NMR diffusion and relaxation measurements are applied to the study of the interaction between the anti-inflammatory drug salicylate and the human serum albumin (HSA) in solutions. The self-diffusion coefficients and the spin-lattice relaxation rates of salicylate are measured as a function of the concentration. The dissociation constant, Kd, for drug/HSA complexes and the number of binding sites, n, are evaluated.
Luo
R S
RS
Liu
M L
ML
Mao
X A
XA
D000894:Anti-Inflammatory Agents, Non-Steroidal / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D004058:Diffusion; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D004364:Pharmaceutical Preparations / Q000737:chemistry / Q000378:metabolism; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*; D012980:Sodium Salicylate / Q000737:chemistry / Q000378:metabolism*; D012996:Solutions
D000894:Anti-Inflammatory Agents, Non-Steroidal; D004364:Pharmaceutical Preparations; D011506:Proteins; D012709:Serum Albumin; D012996:Solutions; D012980:Sodium Salicylate