Mechanism of inactivation of hepatitis B surface antigen by N(α)-cocoyl-L-arginine ethyl ester

Y. Sugimoto, S. Toyoshima

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

The mechanism of N(a)-cocoyl-L-arginine ethyl ester (CAE) in the inactivation of hepatitis B surface antigen (HBsAg) was investigated. The CAE increased the density of HBsAg, and particles of the antigen were destroyed in amorphous clusters, suggesting that CAE influences the lipid components of HBsAg. The lipid components such as cholesterol and phospholipid were mostly removed from the antigen by the treatment with CAE. N(α)-Lauroyl-L[U14C] arginine ethyl ester (LAE), a principal component of CAE, became tightly bound to HBsAg in place of the lipid components. The binding amounts of LAE in the HBsAg-LAE complex reached 3.04 ± 0.44 μg/mg of protein. The formation of the complex was not influenced by the presence of CAE-related compounds such as L-arginine, L-arginine ethyl ester, and N(α)-cocoyl-L-arginine. Treatment with mercaptoethanol-urea, guanidine hydrochloride, and some detergents failed to resolve appreciably the labeled LAE from the labeled complex. All attempts to reactivate the CAE-treated HBsAg and to restore it morphologically from the denatured aggregates were unsuccessful. These results indicate that CAE tightly binds to HBsAg, followed by formation of stable aggregates of the denatured HBsAg-CAE complex.

Original languageEnglish
Pages (from-to)120-127
Number of pages8
JournalAntimicrobial Agents and Chemotherapy
Volume20
Issue number1
DOIs
Publication statusPublished - 1981

ASJC Scopus subject areas

  • Pharmacology
  • Pharmacology (medical)
  • Infectious Diseases

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