ArticleProceedings of the National Academy of Sciences of the United States of America2003
Protein grafting of an HIV-1-inhibiting epitope.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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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
20 citing papers in PubMed, 57 citations in OpenAlex.
- Article
- Bringing immunofocusing into focus.NPJ vaccines · 2024Review
- A glutamine-based single α-helix scaffold to target globular proteins.Nature communications · 2022Article
- Exploring the binding of rationally engineered tandem-repeat proteins to E3 ubiquitin ligase Keap1.Protein engineering, design & selection : PEDS · 2021Article
- Exploring new strategies for grafting binding peptides onto protein loops using a consensus-designed tetratricopeptide repeat scaffold.Protein science : a publication of the Protein Society · 2019Article
- Designing macrocyclic disulfide-rich peptides for biotechnological applications.Nature chemical biology · 2018Article
- When the Scaffold Cannot Be Ignored: The Role of the Hydrophobic Core in Ligand Binding and Specificity.Journal of molecular biology · 2015Article
- Computational design and experimental verification of a symmetric protein homodimer.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- GLUE that sticks to HIV: a helix-grafted GLUE protein that selectively binds the HIV gp41 N-terminal helical region.Chembiochem : a European journal of chemical biology · 2015Article
- Motif-directed redesign of enzyme specificity.Protein science : a publication of the Protein Society · 2014Article
- Max Bergmann lecture protein epitope mimetics in the age of structural vaccinology.Journal of peptide science : an official publication of the European Peptide Society · 2013Review
- A multivalent HIV-1 fusion inhibitor based on small helical foldamers.Tetrahedron · 2012Article
- Computational design of high-affinity epitope scaffolds by backbone grafting of a linear epitope.Journal of molecular biology · 2012Article
- Identification of a beta3-peptide HIV fusion inhibitor with improved potency in live cells.Bioorganic & medicinal chemistry letters · 2009Article
- Exploring the molecular design of protein interaction sites with molecular dynamics simulations and free energy calculations.Biochemistry · 2009Article
- Topical application of entry inhibitors as "virustats" to prevent sexual transmission of HIV infection.Retrovirology · 2008Review
- Article
- Nonhelical leash and alpha-helical structures determine the potency of a peptide antagonist of human T-cell leukemia virus entry.Journal of virology · 2008Article
- Inhibiting HIV fusion with a beta-peptide foldamer.Journal of the American Chemical Society · 2005Article
- gp41: HIV's shy protein.Nature medicine · 2004Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Protein grafting, the transfer of a binding epitope of one ligand onto the surface of another protein, is a potentially powerful technique for presenting peptides in preformed and active three-dimensional conformations. Its utility, however, has been limited by low biological activity of the designed ligands and low tolerance of the protein scaffolds to surface substitutions. Here, we graft the complete binding epitope (19 nonconsecutive amino acids with a solvent-accessible surface area of >2,000 A2) of an HIV-1 C-peptide, which is derived from the C-terminal region of HIV-1 gp41 and potently inhibits HIV-1 entry into cells, onto the surface of a GCN4 leucine zipper. The designed peptide, named C34coil, displays a potent antiviral activity approaching that of the native ligand. Moreover, whereas the linear C-peptide is unstructured and sensitive to degradation by proteases, C34coil is well structured, conformationally stable, and exhibits increased resistance to proteolytic degradation compared with the linear peptide. In addition to being a structured antiviral inhibitor, C34coil may also serve as the basis for the development of an alternative class of immunogens. This study demonstrates that "one-shot" protein grafting, without subsequent rounds of optimization, can be used to create ligands with structural conformations and improved biomedical properties.
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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.