Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation

doi:10.1146/annurev-physchem-050317-021322

Review

. 2018 Apr 20:69:273-298.

doi: 10.1146/annurev-physchem-050317-021322. Epub 2018 Feb 28.

Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation

Thomas C T Michaels^{1

2}, Anđela Šarić³, Johnny Habchi¹, Sean Chia¹, Georg Meisl¹, Michele Vendruscolo¹, Christopher M Dobson¹, Tuomas P J Knowles^{1

4}

Affiliations

¹ Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom; email: [email protected].
² Paulson School of Engineering and Applied Sciences, Harvard University, Cambridge, Massachusetts 02138, USA.
³ Department of Physics and Astronomy, and Institute for the Physics of Living Systems, University College London, London WC1E 6BT, United Kingdom.
⁴ Cavendish Laboratory, Department of Physics, University of Cambridge, Cambridge CB3 1HE, United Kingdom; email: [email protected] , [email protected].

PMID: 29490200
DOI: 10.1146/annurev-physchem-050317-021322

Review

Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation

Thomas C T Michaels et al. Annu Rev Phys Chem. 2018.

. 2018 Apr 20:69:273-298.

doi: 10.1146/annurev-physchem-050317-021322. Epub 2018 Feb 28.

Authors

Thomas C T Michaels^{1

2}, Anđela Šarić³, Johnny Habchi¹, Sean Chia¹, Georg Meisl¹, Michele Vendruscolo¹, Christopher M Dobson¹, Tuomas P J Knowles^{1

4}

Affiliations

¹ Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom; email: [email protected].
² Paulson School of Engineering and Applied Sciences, Harvard University, Cambridge, Massachusetts 02138, USA.
³ Department of Physics and Astronomy, and Institute for the Physics of Living Systems, University College London, London WC1E 6BT, United Kingdom.
⁴ Cavendish Laboratory, Department of Physics, University of Cambridge, Cambridge CB3 1HE, United Kingdom; email: [email protected] , [email protected].

PMID: 29490200
DOI: 10.1146/annurev-physchem-050317-021322

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.

Keywords: Alzheimer's disease; coarse-grained simulations; computer simulations; drug discovery; global fit; inhibition; master equation; neurodegenerative diseases; oligomers; protein aggregation; protein misfolding; rate law; reaction order; scaling exponent; secondary nucleation; self-assembly.

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Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation

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Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation

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