Isolation of HIV-1 protease-inhibiting peptides from thermolysin hydrolysate of oyster proteins

Biochem Biophys Res Commun. 1998 Dec 30;253(3):604-8. doi: 10.1006/bbrc.1998.9824.

Abstract

The peptides inhibiting HIV-1 protease were isolated from the hydrolysate of oyster (Crassostrea gigas) proteins prepared with thermolysin. The amino acid sequences of the peptides were determined as Leu-Leu-Glu-Tyr-Ser-Ile and Leu-Leu-Glu-Tyr-Ser-Leu. These sequences exist in some proteins of variola major virus or human cytomegalovirus. Chemically synthesized Leu-Leu-Glu-Tyr-Ser-Ile and Leu-Leu-Glu-Tyr-Ser-Leu showed IC50 values of 20 and 15 nM, respectively, and behaved as competitive inhibitors for HIV-1 protease with Ki values of 13 and 10 nM, respectively. These peptides were more potent as an HIV-1 protease inhibitor than pepstatin A.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • HIV Protease Inhibitors / isolation & purification*
  • HIV-1*
  • Hydrolysis
  • Ostreidae*
  • Pepstatins / pharmacology
  • Peptides / isolation & purification*
  • Thermolysin / metabolism

Substances

  • HIV Protease Inhibitors
  • Pepstatins
  • Peptides
  • Streptomyces pepsin inhibitor
  • Thermolysin
  • pepstatin