Acetylsalicylate-human serum albumin interaction as studied by nmr spectroscopy-antigenicity-producing mechanism of acetylsalicylic acid

Honma Keishin, Nakamura Mikio, Ishikawa Youichi

Research output: Contribution to journalArticle

22 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)107-113
Number of pages7
JournalMolecular Immunology
Volume28
Issue number1-2
DOIs
Publication statusPublished - 1991

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Serum Albumin
Aspirin
Spectrum Analysis
Salicylates
Human Activities
Salicylic Acid
Esterases
Drug Interactions
Protons
Hydrolysis
Magnetic Resonance Spectroscopy
Pharmaceutical Preparations

ASJC Scopus subject areas

  • Molecular Biology
  • Immunology

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Acetylsalicylate-human serum albumin interaction as studied by nmr spectroscopy-antigenicity-producing mechanism of acetylsalicylic acid. / Keishin, Honma; Mikio, Nakamura; Youichi, Ishikawa.

In: Molecular Immunology, Vol. 28, No. 1-2, 1991, p. 107-113.

Research output: Contribution to journalArticle

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