ArticleJournal of the American Chemical Society2019
Transition of Metastable Cross-α Crystals into Cross-β Fibrils by β-Turn Flipping.
Article in Journal of the American Chemical Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Enhancing the Antimicrobial Potency of Self-Assembling Antibiotics by Co-Assembly-Based Aggregation Modulation.Macromolecular bioscience · 2026Article
- RobustSmall science · 2025Article
- ExploreTurns: A web tool for the exploration, analysis, and classification of beta turns and structured loops in proteins; application to beta-bulge and Schellman loops, Asx helix caps, beta hairpins, and other hydrogen-bonded motifs.Protein science : a publication of the Protein Society · 2025Article
- Unidirectional rotation of micromotors on water powered by pH-controlled disassembly of chiral molecular crystals.Nature communications · 2023Article
- Rational design and topochemical synthesis of polymorphs of a polymer.Chemical science · 2023Article
- Differential fibril morphologies and thermostability determine functional roles ofFrontiers in molecular biosciences · 2023Article
- Single-crystal-to-single-crystal translation of a helical supramolecular polymer to a helical covalent polymer.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The amphibian antimicrobial peptide uperin 3.5 is a cross-α/cross-β chameleon functional amyloid.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Modulation of Amyloidogenic Protein Self-Assembly Using Tethered Small Molecules.Journal of the American Chemical Society · 2020Article
- The substitution of a single amino acid with its enantiomer for control over the adjuvant activity of self-assembling peptides.RSC advances · 2020Article
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Authors and funding
11 authors.
Funding
Abstract
The ensemble of native, folded state was once considered to represent the global energy minimum of a given protein sequence. More recently, the discovery of the cross-β amyloid state revealed that deeper energy minima exist, often associated with pathogenic, fibrillar deposits, when the concentration of proteins reaches a critical value. Fortunately, a sizable energy barrier impedes the conversion from native to pathogenic states. However, little is known about the structure of the related transition state. In addition, there are indications of polymorphism in the amyloidogenic process. Here, we report the first evidence of the conversion of metastable cross-α-helical crystals to thermodynamically stable cross-β-sheet-like fibrils by a de novo designed heptapeptide. Furthermore, for the first time, we demonstrate at atomic resolution that the flip of a peptide plane from a type I to a type II' turn facilitates transformation to cross-β structure and assembly of a dry steric zipper. This study establishes the potential of a peptide turn, a common protein secondary structure, to serve as a principal gatekeeper between a native metastable folded state and the amyloid state.
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