ArticleAntimicrobial agents and chemotherapy2012
Antiviral breadth and combination potential of peptide triazole HIV-1 entry inhibitors.
Article in Antimicrobial agents and chemotherapy, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- Conformational activation and disulfide exchange in HIV-1 Env induce cell-free lytic/fusogenic transformation and enhance infection.Journal of virology · 2025Article
- A Literature Review Focusing on the Antiviral Activity of [1,2,4] and [1,2,3]-triazoles.Mini reviews in medicinal chemistry · 2024Review
- Synthesis of Novel Aminothiazole Derivatives as Promising Antiviral, Antioxidant and Antibacterial Candidates.International journal of molecular sciences · 2022Article
- Peptide-Based HIV Entry Inhibitors.Advances in experimental medicine and biology · 2022Article
- Altered Env conformational dynamics as a mechanism of resistance to peptide-triazole HIV-1 inactivators.Retrovirology · 2021Article
- Peptide Triazole Thiol Irreversibly Inactivates Metastable HIV-1 Env by Accessing Conformational Triggers Intrinsic to Virus-Cell Entry.Microorganisms · 2021Article
- Triazole-Modified Peptidomimetics: An Opportunity for Drug Discovery and Development.Frontiers in chemistry · 2021Review
- Pharmacokinetic stability of macrocyclic peptide triazole HIV-1 inactivators alone and in liposomes.Journal of peptide science : an official publication of the European Peptide Society · 2019Article
- Bifunctional Chimera That Coordinately Targets Human Immunodeficiency Virus 1 Envelope gp120 and the Host-Cell CCR5 Coreceptor at the Virus-Cell Interface.Journal of medicinal chemistry · 2018Article
- Targeting cell surface HIV-1 Env protein to suppress infectious virus formation.Virus research · 2017Article
- Recognition of HIV-inactivating peptide triazoles by the recombinant soluble Env trimer, BG505 SOSIP.664.Proteins · 2017Article
- Short Communication: Inhibition of DC-SIGN-Mediated HIV-1 Infection by Complementary Actions of Dendritic Cell Receptor Antagonists and Env-Targeting Virus Inactivators.AIDS research and human retroviruses · 2016Article
- Disulfide Sensitivity in the Env Protein Underlies Lytic Inactivation of HIV-1 by Peptide Triazole Thiols.ACS chemical biology · 2015Article
- Macrocyclic Envelope Glycoprotein Antagonists that Irreversibly Inactivate HIV-1 before Host Cell Encounter.Journal of medicinal chemistry · 2015Article
- Peptide Triazole Inactivators of HIV-1 Utilize a Conserved Two-Cavity Binding Site at the Junction of the Inner and Outer Domains of Env gp120.Journal of medicinal chemistry · 2015Article
- Mechanism of multivalent nanoparticle encounter with HIV-1 for potency enhancement of peptide triazole virus inactivation.The Journal of biological chemistry · 2015Article
- Peptide triazole inactivators of HIV-1: how do they work and what is their potential?Future medicinal chemistry · 2015Article
- Covalent conjugation of a peptide triazole to HIV-1 gp120 enables intramolecular binding site occupancy.Biochemistry · 2014Article
- Interactions of peptide triazole thiols with Env gp120 induce irreversible breakdown and inactivation of HIV-1 virions.Retrovirology · 2013Article
- A model of peptide triazole entry inhibitor binding to HIV-1 gp120 and the mechanism of bridging sheet disruption.Biochemistry · 2013Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
Abstract
The first stage of human immunodeficiency virus type 1 (HIV-1) infection involves the fusion of viral and host cellular membranes mediated by viral envelope glycoprotein gp120. Inhibitors that specifically target gp120 are gaining increased attention as therapeutics or preventatives to prevent the spread of HIV-1. One promising new group of inhibitors is the peptide triazoles, which bind to gp120 and simultaneously block its interaction with both CD4 and the coreceptor. In this study, we assessed the most potent peptide triazole, HNG-156, for inhibitory breadth, cytotoxicity, and efficacy, both alone and in combination with other antiviral compounds, against HIV-1. HNG-156 inhibited a panel of 16 subtype B and C isolates of HIV-1 in a single-round infection assay. Inhibition of cell infection by replication-competent clinical isolates of HIV-1 was also observed with HNG-156. We found that HNG-156 had a greater than predicted effect when combined with several other entry inhibitors or the reverse transcriptase inhibitor tenofovir. Overall, we find that HNG-156 is noncytotoxic, has a broad inhibition profile, and provides a positive combination with several inhibitors of the HIV-1 life cycle. These results support the pursuit of efficacy and toxicity analyses in more advanced cell and animal models to develop peptide triazole family inhibitors of HIV-1 into antagonists of HIV-1 infection.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.