ArticleMolecules (Basel, Switzerland)2019
Rippled β-Sheet Formation by an Amyloid-β Fragment Indicates Expanded Scope of Sequence Space for Enantiomeric β-Sheet Peptide Coassembly.
Article in Molecules (Basel, Switzerland), 2019. 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, 35 citations in OpenAlex.
- Co-assembly and self-sorting are not mutually exclusive in enantiomeric peptide systems.Chemical science · 2026Article
- Comparison of Pleated and Rippled β-Sheet Assembly of Sequence Isomers of an Amphipathic Self-Assembling Peptide.Biochemistry · 2026Article
- The Rippled Beta-Sheet: An Old Prediction Inspires a New Field.Chembiochem : a European journal of chemical biology · 2026Review
- Unraveling the Atomistic Mechanism of Electrostatic Lateral Association of Peptide β-Sheet Structures and Its Role in Nanofiber Growth and Hydrogelation.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Peptide and Protein Stereocomplexes.ACS omega · 2024Review
- The rippled β-sheet layer configuration-a novel supramolecular architecture based on predictions by Pauling and Corey.Chemical science · 2022Article
- Enantiomeric β-sheet peptides from Aβ form homochiral pleated β-sheets rather than heterochiral rippled β-sheets.Chemical science · 2022Article
- Biomaterials via peptide assembly: Design, characterization, and application in tissue engineering.Acta biomaterialia · 2022Review
- A crystal-structural study of Pauling-Corey rippled sheets.Chemical science · 2022Article
- Understanding and controlling amyloid aggregation with chirality.Current opinion in chemical biology · 2021Review
- Comparisons of β-Hairpin Propensity Among Peptides with Homochiral or Heterochiral Strands.Chembiochem : a European journal of chemical biology · 2021Article
- Constraints on the Structure of Fibrils Formed by a Racemic Mixture of Amyloid-β Peptides from Solid-State NMR, Electron Microscopy, and Theory.Journal of the American Chemical Society · 2021Article
- Autofluorescence of Amyloids Determined by Enantiomeric Composition of Peptides.The journal of physical chemistry. B · 2021Article
- Defining the Landscape of the Pauling-Corey Rippled Sheet: An Orphaned Motif Finding New Homes.Accounts of chemical research · 2021Review
- Charge guides pathway selection in β-sheet fibrillizing peptide co-assembly.Communications chemistry · 2020Article
- Synergistic Interactions Are Prevalent in Catalytic Amyloids.Chembiochem : a European journal of chemical biology · 2020Article
- Editorial to the Special Issue-"Recent Advances in Self-Assembled Peptides".Molecules (Basel, Switzerland) · 2019Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
In 1953, Pauling and Corey predicted that enantiomeric β-sheet peptides would coassemble into so-called "rippled" β-sheets, in which the β-sheets would consist of alternating l- and d-peptides. To date, this phenomenon has been investigated primarily with amphipathic peptide sequences composed of alternating hydrophilic and hydrophobic amino acid residues. Here, we show that enantiomers of a fragment of the amyloid-β (Aβ) peptide that does not follow this sequence pattern, amyloid-β (16-22), readily coassembles into rippled β-sheets. Equimolar mixtures of enantiomeric amyloid-β (16-22) peptides assemble into supramolecular structures that exhibit distinct morphologies from those observed by self-assembly of the single enantiomer pleated β-sheet fibrils. Formation of rippled β-sheets composed of alternating l- and d-amyloid-β (16-22) is confirmed by isotope-edited infrared spectroscopy and solid-state NMR spectroscopy. Sedimentation analysis reveals that rippled β-sheet formation by l- and d-amyloid-β (16-22) is energetically favorable relative to self-assembly into corresponding pleated β-sheets. This work illustrates that coassembly of enantiomeric β-sheet peptides into rippled β-sheets is not limited to peptides with alternating hydrophobic/hydrophilic sequence patterns, but that a broader range of sequence space is available for the design and preparation of rippled β-sheet materials.
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