title: Acetylsalicylate-human serum albumin interaction as studied by NMR spectroscopy--antigenicity-producing mechanism of acetylsalicylic acid.
abstract: To discover the antigenicity-producing mechanism of acetylsalicylic acid, the interaction of this drug and relevant salicylic acid with human serum albumin (HSA) has been studied by means of nuclear magnetic resonance (NMR) spectroscopy. The determination of spin-lattice relaxation rates (1/T1) of some protons have revealed that one HSA molecule can bind acetylsalicylate and salicylate up to 80 and 290 molecules, respectively. The hydrolysis rates of acetylsalicylate were greatly enhanced in the presence of HSA, especially when the drug/HSA mole ratio was small. Thus, the esterase-like activity of HSA was verified. This activity of HSA was effectively inhibited by salicylate; the effect was ascribed to the stronger binding affinity of salicylate toward HSA as compared with that of acetylsalicylate. Based on these results, the antigenicity-producing mechanism of acetylsalicylate and salicylate has been discussed.
authors.affiliation: Department of Immunology, Toho University School of Medicine, Tokyo, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Honma
authors.forename: M
authors.initials: M
authors.lastname: Nakamura
authors.forename: Y
authors.initials: Y
authors.lastname: Ishikawa
mesh_terms: D001241:Aspirin / Q000737:chemistry* / Q000276:immunology; D006801:Humans; D066298:In Vitro Techniques; D009682:Magnetic Resonance Spectroscopy; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry*
chemical_list: D012709:Serum Albumin; D001241:Aspirin