ArticleJournal of molecular biology2011
Design of peptide inhibitors that bind the bZIP domain of Epstein-Barr virus protein BZLF1.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The trial behind it
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Article
- Computational Tools and Strategies to Develop Peptide-Based Inhibitors of Protein-Protein Interactions.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Selective antagonism of cJun for cancer therapy.Journal of experimental & clinical cancer research : CR · 2020Review
- Designing helical peptide inhibitors of protein-protein interactions.Current opinion in structural biology · 2016Review
- Data-driven prediction and design of bZIP coiled-coil interactions.PLoS computational biology · 2015Article
- A set of computationally designed orthogonal antiparallel homodimers that expands the synthetic coiled-coil toolkit.Journal of the American Chemical Society · 2014Article
- Increasing the affinity of selective bZIP-binding peptides through surface residue redesign.Protein science : a publication of the Protein Society · 2014Article
- Strategies to control the binding mode of de novo designed protein interactions.Current opinion in structural biology · 2013Review
- Article
- Designing specific protein-protein interactions using computation, experimental library screening, or integrated methods.Protein science : a publication of the Protein Society · 2012Review
- The d'--d--d' vertical triad is less discriminating than the a'--a--a' vertical triad in the antiparallel coiled-coil dimer motif.Journal of the American Chemical Society · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Designing proteins or peptides that bind native protein targets can aid the development of novel reagents and/or therapeutics. Rational design also tests our understanding of the principles underlying protein recognition. This article describes several strategies used to design peptides that bind to the basic region leucine zipper (bZIP) domain of the viral transcription factor BZLF1, which is encoded by the Epstein-Barr virus. BZLF1 regulates the transition of the Epstein-Barr virus from a latent state to a lytic state. It shares some properties in common with the more studied human bZIP transcription factors, but also includes novel structural elements that pose interesting challenges to inhibitor design. In designing peptides that bind to BZLF1 by forming a coiled-coil structure, we considered both affinity for BZLF1 and undesired self-association, which can weaken the effectiveness of an inhibitor. Several designed peptides exhibited different degrees of target-binding affinity and self-association. Rationally engineered molecules were more potent inhibitors of DNA binding than a control peptide corresponding to the native BZLF1 dimerization region itself. The most potent inhibitors included both positive and negative design elements and exploited interaction with the coiled-coil and basic DNA-binding regions of BZLF1.
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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.