Polymorphism in an amyloid-like fibril-forming model peptide

René Verel, Ivan T. Tomka, Carlo Bertozzi, Riccardo Cadalbert, Richard A. Kammerer, Michel O. Steinmetz, Beat H. Meier

    Research output: Contribution to journalArticlepeer-review


    (Figure Presented) The structural basis for polymorphism in amyloids is unraveled with a model system. The hydrogen-bonding pattern within the β sheets of fibrils is strongly influenced by the pH of the solution from which the fibrils are formed. Solid-state NMR spectroscopy experiments allow quantification of the relative amounts of two different β-sheet structures over the pH range 2.0-7.3. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.
    Original languageEnglish
    Pages (from-to)5842-5845
    Number of pages3
    JournalAngewandte Chemie - International Edition
    Issue number31
    Publication statusPublished - 21 Jul 2008


    • Fibrils
    • NMR spectroscopy
    • Peptides
    • Protein structures
    • Structural biology


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