title: Statine based tripeptides as potent inhibitors of HIV-1 replication.
abstract: Starting from highly potent HIV-1 protease pepstatine analog inhibitors, we have tried to find the minimum consensus sequence which is necessary to conserve anti-protease potency and antiviral activity. We describe here some statine based tripeptides which exhibit high affinity for the protease and are able to inhibit the reproductive cycle of HIV-1 in MT-4-infected cells.
authors.affiliation: Sanofi Recherche, Montpellier, France.
authors.forename: J A
authors.initials: JA
authors.lastname: Fehrentz
authors.forename: B
authors.initials: B
authors.lastname: Chomier
authors.forename: E
authors.initials: E
authors.lastname: Bignon
authors.forename: S
authors.initials: S
authors.lastname: Venaud
authors.forename: J C
authors.initials: JC
authors.lastname: Chermann
authors.forename: D
authors.initials: D
authors.lastname: Nisato
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000494:pharmacology*; D002460:Cell Line; D016333:HIV Protease / Q000378:metabolism*; D017320:HIV Protease Inhibitors / Q000138:chemical synthesis / Q000494:pharmacology*; D015497:HIV-1 / Q000187:drug effects* / Q000502:physiology; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000494:pharmacology*; D013329:Structure-Activity Relationship; D014779:Virus Replication / Q000187:drug effects*
chemical_list: D000596:Amino Acids; D017320:HIV Protease Inhibitors; D009842:Oligopeptides; D016333:HIV Protease; C013165:statine