A clear view of polymorphism, twist, and chirality in amyloid fibril formation

Lisa R. Volpatti, Michele Vendruscolo, Christopher M. Dobson, Tuomas P.J. Knowles*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

81 Scopus citations

Abstract

The self-assembly of protein molecules into highly ordered linear aggregates, known as amyloid fibrils, is a phenomenon receiving increasing attention because of its biological roles in health and disease and the potential of these structures to form artificial proteinaceous scaffolds for biomaterials applications. A particularly powerful approach to probe the key physical properties of fibrillar structures is atomic force microscopy, which was used by Usov et al. in this issue of ACS Nano to reveal the polymorphic transitions and chirality inversions of amyloid fibrils in unprecedented detail. Starting from this study, this Perspective highlights recent progress in understanding the dynamic polymorphism, twisting behavior, and handedness of amyloid fibrils and discusses the promising future of these self-assembling structures as advanced functional materials with applications in nanotechnology and related fields.

Original languageEnglish (US)
Pages (from-to)10443-10448
Number of pages6
JournalACS nano
Volume7
Issue number12
DOIs
StatePublished - Dec 23 2013
Externally publishedYes

ASJC Scopus subject areas

  • General Materials Science
  • General Engineering
  • General Physics and Astronomy

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