ArticleProceedings of the National Academy of Sciences of the United States of America2017
De novo design of covalently constrained mesosize protein scaffolds with unique tertiary structures.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 74 citations in OpenAlex.
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- CYCLICCAE: A CONFORMATIONAL AUTOENCODER FOR EFFICIENT HETEROCHIRAL MACROCYCLIC BACKBONE SAMPLING.bioRxiv : the preprint server for biology · 2025Article
- Tackling Undruggable Targets with Designer Peptidomimetics and Synthetic Biologics.Chemical reviews · 2024Review
- De novo design of monomeric helical bundles for pH-controlled membrane lysis.Protein science : a publication of the Protein Society · 2023Article
- Mismatched covalent and noncovalent templating leads to large coiled coil-templated macrocycles.Chemical science · 2023Article
- Design and Engineering of Miniproteins.ACS bio & med chem Au · 2022Review
- Multivalent designed proteins neutralize SARS-CoV-2 variants of concern and confer protection against infection in mice.Science translational medicine · 2022Article
- Reconfigurable asymmetric protein assemblies through implicit negative design.Science (New York, N.Y.) · 2022Article
- Protein Macrocyclization for Tertiary Structure Stabilization.Chembiochem : a European journal of chemical biology · 2021Review
- Multivalent designed proteins protect against SARS-CoV-2 variants of concern.bioRxiv : the preprint server for biology · 2021Article
- Transferrin receptor targeting by de novo sheet extension.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Dynamic Stereoselection of Peptide Helicates and Their Selective Labeling of DNA Replication Foci in Cells*.Angewandte Chemie (International ed. in English) · 2021Article
- A library of coiled-coil domains: from regular bundles to peculiar twists.Bioinformatics (Oxford, England) · 2021Article
- Computationally designed peptide macrocycle inhibitors of New Delhi metallo-β-lactamase 1.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Acyl Transfer Catalytic Activity in De Novo Designed Protein with N-Terminus of α-Helix As Oxyanion-Binding Site.Journal of the American Chemical Society · 2021Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
The folding of natural proteins typically relies on hydrophobic packing, metal binding, or disulfide bond formation in the protein core. Alternatively, a 3D structure can be defined by incorporating a multivalent cross-linking agent, and this approach has been successfully developed for the selection of bicyclic peptides from large random-sequence libraries. By contrast, there is no general method for the de novo computational design of multicross-linked proteins with predictable and well-defined folds, including ones not found in nature. Here we use Rosetta and Tertiary Motifs (TERMs) to design small proteins that fold around multivalent cross-linkers. The hydrophobic cross-linkers stabilize the fold by macrocyclic restraints, and they also form an integral part of a small apolar core. The designed CovCore proteins were prepared by chemical synthesis, and their structures were determined by solution NMR or X-ray crystallography. These mesosized proteins, lying between conventional proteins and small peptides, are easily accessible either through biosynthetic precursors or chemical synthesis. The unique tertiary structures and ease of synthesis of CovCore proteins indicate that they should provide versatile templates for developing inhibitors of protein-protein interactions.
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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.