ArticleThe Journal of biological chemistry2008
Solution structure of a hydrocarbon stapled peptide inhibitor in complex with monomeric C-terminal domain of HIV-1 capsid.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 85 citations in OpenAlex.
- Review
- Rotten to the core: antivirals targeting the HIV-1 capsid core.Retrovirology · 2021Review
- The Role of Capsid in the Early Steps of HIV-1 Infection: New Insights into the Core of the Matter.Viruses · 2021Review
- Peptide-based inhibitors of protein-protein interactions: biophysical, structural and cellular consequences of introducing a constraint.Chemical science · 2021Review
- Structure, Function, and Interactions of the HIV-1 Capsid Protein.Life (Basel, Switzerland) · 2021Review
- Incorporation of α-methylated amino acids into Apolipoprotein A-I mimetic peptides improves their helicity and cholesterol efflux potential.Biochemical and biophysical research communications · 2020Article
- Recent Advances in HIV-1 Gag Inhibitor Design and Development.Molecules (Basel, Switzerland) · 2020Review
- Versatile Peptide Macrocyclization with Diels-Alder Cycloadditions.Journal of the American Chemical Society · 2019Article
- Multiple Roles of HIV-1 Capsid during the Virus Replication Cycle.Virologica Sinica · 2019Review
- A Targeted Bivalent Androgen Receptor Binding Compound for Prostate Cancer Therapy.Hormones & cancer · 2019Article
- Stapled Peptides Inhibitors: A New Window for Target Drug Discovery.Computational and structural biotechnology journal · 2019Review
- Inhibitors of the HIV-1 capsid, a target of opportunity.Current opinion in HIV and AIDS · 2018Review
- IKKγ-Mimetic Peptides Block the Resistance to Apoptosis Associated with Kaposi's Sarcoma-Associated Herpesvirus Infection.Journal of virology · 2017Article
- Stapled peptide inhibitors of RAB25 target context-specific phenotypes in cancer.Nature communications · 2017Article
- Identification of a small molecule HIV-1 inhibitor that targets the capsid hexamer.Bioorganic & medicinal chemistry letters · 2016Article
- HIV-1 Capsid Inhibitors as Antiretroviral Agents.Current HIV research · 2016Review
- HIV-1 Gag as an Antiviral Target: Development of Assembly and Maturation Inhibitors.Current topics in medicinal chemistry · 2016Review
- HIV-1 gag: an emerging target for antiretroviral therapy.Current topics in microbiology and immunology · 2015Review
- Cullin3-BTB interface: a novel target for stapled peptides.PloS one · 2015Article
- Z-Selective olefin metathesis on peptides: investigation of side-chain influence, preorganization, and guidelines in substrate selection.Journal of the American Chemical Society · 2014Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The human immunodeficiency virus type 1 (HIV-1) capsid protein plays a critical role in virus core particle assembly and is an important target for novel therapeutic strategies. In a previous study, we characterized the binding affinity of a hydrocarbon stapled helical peptide, NYAD-1, for the capsid protein (K(d) approximately 1 mum) and demonstrated its ability to penetrate the cell membrane (Zhang, H., Zhao, Q., Bhattacharya, S., Waheed, A. A., Tong, X., Hong, A., Heck, S., Goger, M., Cowburn, D., Freed, E. O., and Debnath, A. K. (2008) J. Mol. Biol. 378, 565-580). In cell-based assays, NYAD-1 colocalized with the Gag polyprotein during traffic to the plasma membrane and disrupted the formation of mature and immature virus particles in vitro systems. Here, we complement the cellular and biochemical data with structural characterization of the interactions between the capsid and a soluble peptide analogue, NYAD-13. Solution NMR methods were used to determine a high resolution structure of the complex between the inhibitor and a monomeric form of the C-terminal domain of the capsid protein (mCA-CTD). The intermolecular interactions are mediated by the packing of hydrophobic side chains at the buried interface and unperturbed by the presence of the olefinic chain on the solvent-exposed surface of the peptide. The results of the structural analysis provide valuable insight into the determinants for high affinity and selective inhibitors for HIV-1 particle assembly.
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Registered trials
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