ArticleProtein science : a publication of the Protein Society2019
Exploring new strategies for grafting binding peptides onto protein loops using a consensus-designed tetratricopeptide repeat scaffold.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 17 citations in OpenAlex.
- Tandem-repeat proteins introduce tuneable properties to engineered biomolecular condensates.Chemical science · 2025Article
- Using a stable protein scaffold to display peptides that bind to alpha-synuclein fibrils.Protein science : a publication of the Protein Society · 2025Article
- Lasso-grafting of macrocyclic peptide pharmacophores yields multi-functional proteins.Nature communications · 2021Article
- Exploring the binding of rationally engineered tandem-repeat proteins to E3 ubiquitin ligase Keap1.Protein engineering, design & selection : PEDS · 2021Article
- Engineering mono- and multi-valent inhibitors on a modular scaffold.Chemical science · 2021Article
- Testing the length limit of loop grafting in a helical repeat protein.Current research in structural biology · 2021Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 4 countries.
Funding
Abstract
Peptide display approaches, in which peptide epitopes of known binding activities are grafted onto stable protein scaffolds, have been developed to constrain the peptide in its bioactive conformation and to enhance its stability. However, peptide grafting can be a lengthy process requiring extensive computational modeling and/or optimisation by directed evolution techniques. In this study, we show that ultra-stable consensus-designed tetratricopeptide repeat (CTPR) proteins are amenable to the grafting of peptides that bind the Kelch-like ECH-associated protein 1 (Keap1) onto the loop between adjacent repeats. We explore simple strategies to optimize the grafting process and show that modest improvements in Keap1-binding affinity can be obtained by changing the composition of the linker sequence flanking either side of the binding peptide.
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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.