ArticleProceedings of the National Academy of Sciences of the United States of America2010
Minimalist design of water-soluble cross-beta architecture.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Bioinformatic assessment of the potential amyloidogenicity of the human and evolutionarily more ancient proteomes.The Biochemical journal · 2026Article
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- AmyloGram reveals amyloidogenic potential in stroke thrombus proteomes.The Biochemical journal · 2025Article
- High-yield spidroin mimics for bioinspired fibers via computational design.Frontiers in bioengineering and biotechnology · 2025Article
- Co-Localized in Amyloid Plaques Cathepsin B as a Source of Peptide Analogs Potential Drug Candidates for Alzheimer's Disease.Biomolecules · 2024Article
- Transthyretin Stabilizers and Seeding Inhibitors as Therapies for Amyloid Transthyretin Cardiomyopathy.Pharmaceutics · 2023Review
- Amyloidogenesis: What Do We Know So Far?International journal of molecular sciences · 2022Review
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- The Possible Mechanism of Amyloid Transformation Based on the Geometrical Parameters of Early-Stage Intermediate in Silico Model for Protein Folding.International journal of molecular sciences · 2022Article
- Amyloid-Like Aggregation in Diseases and Biomaterials: Osmosis of Structural Information.Frontiers in bioengineering and biotechnology · 2021Review
- Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model.International journal of molecular sciences · 2018Article
- Optical Structural Analysis of Individual α-Synuclein Oligomers.Angewandte Chemie (International ed. in English) · 2018Article
- Modeling repetitive, non-globular proteins.Protein science : a publication of the Protein Society · 2016Review
- Article
- Novel dimeric β-helical model of an ice nucleation protein with bridged active sites.BMC structural biology · 2011Article
- β₂-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages.Nature structural & molecular biology · 2011Article
- Protein-induced photophysical changes to the amyloid indicator dye thioflavin T.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
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3 authors.
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Abstract
Demonstrated successes of protein design and engineering suggest significant potential to produce diverse protein architectures and assemblies beyond those found in nature. Here, we describe a new class of synthetic protein architecture through the successful design and atomic structures of water-soluble cross-beta proteins. The cross-beta motif is formed from the lamination of successive beta-sheet layers, and it is abundantly observed in the core of insoluble amyloid fibrils associated with protein-misfolding diseases. Despite its prominence, cross-beta has been designed only in the context of insoluble aggregates of peptides or proteins. Cross-beta's recalcitrance to protein engineering and conspicuous absence among the known atomic structures of natural proteins thus makes it a challenging target for design in a water-soluble form. Through comparative analysis of the cross-beta structures of fibril-forming peptides, we identified rows of hydrophobic residues ("ladders") running across beta-strands of each beta-sheet layer as a minimal component of the cross-beta motif. Grafting a single ladder of hydrophobic residues designed from the Alzheimer's amyloid-beta peptide onto a large beta-sheet protein formed a dimeric protein with a cross-beta architecture that remained water-soluble, as revealed by solution analysis and x-ray crystal structures. These results demonstrate that the cross-beta motif is a stable architecture in water-soluble polypeptides and can be readily designed. Our results provide a new route for accessing the cross-beta structure and expanding the scope of protein design.
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