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Publication Detail
Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Article
  • Authors:
    Michaels TCT, Šarić A, Habchi J, Chia S, Meisl G, Vendruscolo M, Dobson CM, Knowles TPJ
  • Publication date:
    28/02/2018
  • Journal:
    Annual review of physical chemistry
  • Medium:
    Print-Electronic
  • Status:
    Published
  • Print ISSN:
    0066-426X
  • Language:
    eng
  • Addresses:
    Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom; email: tctm3@cam.ac.uk.
Abstract
Understanding how normally soluble peptides and proteins aggregate to form amyloid fibrils is central to many areas of modern biomolecular science, ranging from the development of functional biomaterials to the design of rational therapeutic strategies against increasingly prevalent medical conditions such as Alzheimer's and Parkinson's diseases. As such, there is a great need to develop models to mechanistically describe how amyloid fibrils are formed from precursor peptides and proteins. Here we review and discuss how ideas and concepts from chemical reaction kinetics can help to achieve this objective. In particular, we show how a combination of theory, experiments, and computer simulations, based on chemical kinetics, provides a general formalism for uncovering, at the molecular level, the mechanistic steps that underlie the phenomenon of amyloid fibril formation. Expected final online publication date for the Annual Review of Physical Chemistry Volume 69 is April 20, 2018. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.
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