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NCp7: targeting a multitasking protein for next-generation anti-HIV drug development part 1: covalent inhibitors.

Identifieur interne : 000A67 ( PubMed/Corpus ); précédent : 000A66; suivant : 000A68

NCp7: targeting a multitasking protein for next-generation anti-HIV drug development part 1: covalent inhibitors.

Auteurs : Luca Sancineto ; Nunzio Iraci ; Oriana Tabarrini ; Claudio Santi

Source :

RBID : pubmed:29107765

English descriptors

Abstract

The major internal component of the HIV virion core is the nucleocapsid protein 7 (NCp7), a small, highly basic protein that is essential for multiple stages of the viral replicative cycle, and whose structure is preserved in all viral strains, including clinical isolates from therapy-experienced patients. This key protein is recognised as a potential target for an effective next-generation antiretroviral therapy, because it could offer the possibility to develop broad-spectrum agents that are less prone to select for resistant strains. Here, we provide a comprehensive overview of the covalent NCp7 inhibitors that have emerged over the past 25 years of drug discovery campaigns, emphasising, where possible, their structure-activity relationships (SARs) and pharmacophoric features.

DOI: 10.1016/j.drudis.2017.10.017
PubMed: 29107765

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pubmed:29107765

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<div type="abstract" xml:lang="en">The major internal component of the HIV virion core is the nucleocapsid protein 7 (NCp7), a small, highly basic protein that is essential for multiple stages of the viral replicative cycle, and whose structure is preserved in all viral strains, including clinical isolates from therapy-experienced patients. This key protein is recognised as a potential target for an effective next-generation antiretroviral therapy, because it could offer the possibility to develop broad-spectrum agents that are less prone to select for resistant strains. Here, we provide a comprehensive overview of the covalent NCp7 inhibitors that have emerged over the past 25 years of drug discovery campaigns, emphasising, where possible, their structure-activity relationships (SARs) and pharmacophoric features.</div>
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