Literature DB >> 29490200

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

Thomas C T Michaels1,2, Anđela Šarić3, Johnny Habchi1, Sean Chia1, Georg Meisl1, Michele Vendruscolo1, Christopher M Dobson1, Tuomas P J Knowles1,4.   

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.

Entities:  

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

Mesh:

Substances:

Year:  2018        PMID: 29490200     DOI: 10.1146/annurev-physchem-050317-021322

Source DB:  PubMed          Journal:  Annu Rev Phys Chem        ISSN: 0066-426X            Impact factor:   12.703


  41 in total

1.  Amyloid found in human cataracts with two-dimensional infrared spectroscopy.

Authors:  Ariel M Alperstein; Joshua S Ostrander; Tianqi O Zhang; Martin T Zanni
Journal:  Proc Natl Acad Sci U S A       Date:  2019-03-20       Impact factor: 11.205

2.  Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors.

Authors:  Thomas C T Michaels; Andela Šarić; Georg Meisl; Gabriella T Heller; Samo Curk; Paolo Arosio; Sara Linse; Christopher M Dobson; Michele Vendruscolo; Tuomas P J Knowles
Journal:  Proc Natl Acad Sci U S A       Date:  2020-09-14       Impact factor: 11.205

3.  Amyloid assembly is dominated by misregistered kinetic traps on an unbiased energy landscape.

Authors:  Zhiguang Jia; Jeremy D Schmit; Jianhan Chen
Journal:  Proc Natl Acad Sci U S A       Date:  2020-04-28       Impact factor: 11.205

4.  Optimal control strategies for inhibition of protein aggregation.

Authors:  Thomas C T Michaels; Christoph A Weber; L Mahadevan
Journal:  Proc Natl Acad Sci U S A       Date:  2019-06-28       Impact factor: 11.205

Review 5.  Interpretable artificial intelligence and exascale molecular dynamics simulations to reveal kinetics: Applications to Alzheimer's disease.

Authors:  William Martin; Gloria Sheynkman; Felice C Lightstone; Ruth Nussinov; Feixiong Cheng
Journal:  Curr Opin Struct Biol       Date:  2021-10-07       Impact factor: 6.809

6.  Multi-eGO: An in silico lens to look into protein aggregation kinetics at atomic resolution.

Authors:  Emanuele Scalone; Luca Broggini; Cristina Visentin; Davide Erba; Fran Bačić Toplek; Kaliroi Peqini; Sara Pellegrino; Stefano Ricagno; Cristina Paissoni; Carlo Camilloni
Journal:  Proc Natl Acad Sci U S A       Date:  2022-06-23       Impact factor: 12.779

Review 7.  The Proteome Folding Problem and Cellular Proteostasis.

Authors:  Evan T Powers; Lila M Gierasch
Journal:  J Mol Biol       Date:  2021-08-13       Impact factor: 6.151

8.  Proline-rich domain of human ALIX contains multiple TSG101-UEV interaction sites and forms phosphorylation-mediated reversible amyloids.

Authors:  Ruben D Elias; Wen Ma; Rodolfo Ghirlando; Charles D Schwieters; Vijay S Reddy; Lalit Deshmukh
Journal:  Proc Natl Acad Sci U S A       Date:  2020-09-11       Impact factor: 11.205

Review 9.  The Amyloid Phenomenon and Its Significance in Biology and Medicine.

Authors:  Christopher M Dobson; Tuomas P J Knowles; Michele Vendruscolo
Journal:  Cold Spring Harb Perspect Biol       Date:  2020-02-03       Impact factor: 10.005

10.  Rationally Designed Bicyclic Peptides Prevent the Conversion of Aβ42 Assemblies Into Fibrillar Structures.

Authors:  Tatsuya Ikenoue; Francesco A Aprile; Pietro Sormanni; Michele Vendruscolo
Journal:  Front Neurosci       Date:  2021-02-25       Impact factor: 4.677

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