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PMID: 2241573 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Archives of virology ·Vol. 114 ·No. 3-4 ·1990-00-00 ·Pages 167-73

Grinde B, Hungnes O, Tjøtta E

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.

MeSH Terms
Amino Acid Sequence Cells, Cultured HIV Protease/metabolism HIV-1/drug effects,enzymology,physiology Molecular Sequence Data Oligopeptides/chemical synthesis,metabolism,pharmacology Protease Inhibitors/chemical synthesis,metabolism,pharmacology Virus Replication/drug effects Zidovudine/pharmacology
Chemicals
Oligopeptides Protease Inhibitors Zidovudine HIV Protease
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Grinde B
Department of Virology, National Institute of Public Health, Oslo, Norway.
Hungnes O
Tjøtta E
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27 references, click to expand
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Article Info
Journal
Archives of virology
Abbr.
Arch Virol
ISSN
0304-8608
DOI
10.1007/BF01310746
Published
1990-00-00
Pages
167-73
Language
English
Region
Austria
NLM ID
7506870
Subset
IM
External Links
PubMed source DOI: 10.1007/BF01310746 View journal details
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