We have reported previously that N(α)-cocoyl-L-arginine ethyl ester (CAE) strongly inactivates hepatitis B surface antigen. Replacement of the L-arginine moiety of CAE by L-lysine did not decrease the HBsAg-inactivating effect of CAE, whereas replacement by some neutral amino acids and L-ornithine decreased it. Esterification of the carboxyl group of N(α)-acyl-L-arginine enhanced its inactivating effect. When the ethyl ester of CAE was converted to an amide group, the effect was appreciably decreased. Modification of the carboxyl group was essential for the inactivation. The effectiveness of N(α)-acyl-L-arginine ethyl ester depends upon the length of the acyl group, with the optimum length for the inactivation of HBsAg being C12 to C14. In addition to CAE, N(α)-lauroyl-L-lysine ethyl ester and N(α)-cocoyl-L-arginine amide were found to be strong inactivators of HBsAg. Significant inactivating effects on HBsAg were not observed in many anionic detergents containing an amino acid. These results suggest that for strongly inactivating HBsAg, a compound should contain a special amino acid, such as L-arginine, and a long acyl group and exhibit a cationic property.
|Number of pages||4|
|Journal||Antimicrobial Agents and Chemotherapy|
|Publication status||Published - 1980|
ASJC Scopus subject areas
- Pharmacology (medical)
- Infectious Diseases