Modified oligopeptides designed to interact with the HIV-1 proteinase inhibit viral replication

Arch Virol. 1990;114(3-4):167-73. doi: 10.1007/BF01310746.

Abstract

The human immunodeficiency virus 1 (HIV-1) codes for a proteinase that cuts viral proteins at specific sites. We have tested 13 modified oligopeptides related to these cleavage sites to see if they inhibit viral replication. To indicate whether a decrease in replication could be due to a general inhibition of cell metabolism, we also measured the effect of the peptides on cellular protein synthesis. Three of the peptides tested (Ac-Gln-Asn-Sta-Val-NH2, Ac-Gln-Asn-Sta-Val-Val-NH2, and Ac-Glu-Asn-Sta-Ile-NH2) inhibited HIV-1 replication at concentrations that did not inhibit protein synthesis. Ac-Gln-Asn-Sta-Val-NH2 was the most potent, causing an approximately 40% decrease in viral replication, measured as the synthesis of HIV-1 antigens and the formation of infectious particles.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cells, Cultured
  • HIV Protease / metabolism*
  • HIV-1 / drug effects*
  • HIV-1 / enzymology
  • HIV-1 / physiology
  • Molecular Sequence Data
  • Oligopeptides / chemical synthesis
  • Oligopeptides / metabolism
  • Oligopeptides / pharmacology*
  • Protease Inhibitors / chemical synthesis
  • Protease Inhibitors / metabolism
  • Protease Inhibitors / pharmacology*
  • Virus Replication / drug effects*
  • Zidovudine / pharmacology

Substances

  • Oligopeptides
  • Protease Inhibitors
  • Zidovudine
  • HIV Protease