Design and synthesis of HIV protease inhibitors. Variations of the carboxy terminus of the HIV protease inhibitor L-682,679

Autor:	I S Sigal, S J deSolms, Zugay Ja, J. M. Wiggins, J. P. Vacca, Samuel L. Graham, J. P. Guare, E A Giuliani, William M. Sanders, Paul L. Darke
Rok vydání:	1991
Předmět:	HIV Antigens medicine.medical_treatment T-Lymphocytes Human immunodeficiency virus (HIV) HIV Core Protein p24 Gene Products gag medicine.disease_cause Virus Replication Antiviral Agents gag Gene Products Human Immunodeficiency Virus Virus Viral Proteins Drug Discovery medicine HIV Protease Inhibitor Humans Protein Precursors Protease Tetrapeptide biology Chemistry Viral Core Proteins Biological activity HIV Protease Inhibitors In vitro Biochemistry Enzyme inhibitor Drug Design biology.protein HIV-1 Molecular Medicine Oligopeptides
Zdroj:	Journal of medicinal chemistry. 34(9)
ISSN:	0022-2623
Popis:	A series of tetrapeptide analogues of 1 (L-682,679), in which the carboxy terminus has been shortened and modified, was prepared and their inhibitory activity measured against the HIV protease in a peptide cleavage assay. Selected examples were tested as inhibitors of virus spread in cell culture. Compound 12 was a 10-fold more potent enzyme inhibitor than 1 in vitro and 30-fold more potent in inhibiting the viral spread in cells.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc8da6dbba186808bacd8b16f0dfec43 https://pubmed.ncbi.nlm.nih.gov/1910089 Zobrazit plný text záznamu