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Research article2014Peer reviewed

Amyloid Fibrils: Formation, Polymorphism, and Inhibition

Härd, Torleif


Amyloid fibrils with cross-beta spine basic architectures are prevalent and stable forms of peptides and proteins. Recent research has provided significant contributions to our understanding of the mechanisms of fibril formation and to the surprising diversity and persistence of structural polymorphism in amyloid fibrils. There have also been successful demonstrations of how molecules can be engineered to inhibit unwanted amyloid formation by different mechanisms. Future research in these areas will include investigations of mechanisms for primary nucleation and the structure of oligomeric intermediates, the general role of secondary nucleation events (autocatalysis), elucidation of the mechanisms and implications of preservation of structural morphology in amyloid propagation, and research into the largely unexplored phenomenon of cross-seeding, by which amyloid fibrils of one species induce the formation of amyloid by another species.

Published in

Journal of Physical Chemistry Letters
2014, Volume: 5, number: 3, pages: 607-614

      SLU Authors

    • Härd, Torleif

      • The Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences

    UKÄ Subject classification

    Physical Chemistry

    Publication identifier


    Permanent link to this page (URI)