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A Lumry−Eyring Nucleated Polymerization Model of Protein Aggregation Kinetics: 1. Aggregation with Pre-Equilibrated Unfolding

Andrews, Jennifer M., Roberts, Christopher J.·2007·The Journal of Physical Chemistry B
DOI 10.1021/jp070212j
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Abstract

A mathematical model is presented of the kinetics of non-native protein aggregation that combines Lumry-Eyring and nucleated polymerization (LENP) descriptions. The LENP model is solved for cases in which aggregation rates are slow compared to folding-unfolding equilibration and is shown to be a generalization of a number of previously proposed nucleation-and-growth models for non-native and native protein aggregation. The model solutions exhibit a number of qualitative kinetic regimes. Each regime has a characteristic set of experimental signatures that are related to the relative rates of growth and nucleation as well as to the threshold size at which aggregates condense to form higher-order structures or other phases. Approximate model solutions provide practical rate equations that can be regressed against typical experimental kinetic data to obtain mechanistic parameters characterizing the aggregation pathway. In all kinetic regimes, it is found that observed rate coefficients (kobs) or half-lives (t50) obtained from extent-of-reaction measurements are convolutions of more than one stage in the pathway unless purely seeded growth occurs. Despite this convolution, the combination of apparent reaction order (time domain) and the scaling of kobs or t50 with initial protein concentration provides a means to determine a value for the dominant nucleus size in each case. Additional information, such as equilibrium unfolding thermodynamics and the limiting aggregate size distrib…

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Metadata

Authors
Andrews, J. M., & Roberts, C. J.
Affiliations
University of Delaware (US)
ORCID
Roberts, Christopher J.
Venue
The Journal of Physical Chemistry B
Publisher
American Chemical Society (ACS)
Published
2007-06-16
Volume
111
Issue
27
Pages
7897-7913
ISSN
  • 1520-5207 (ISSN-L)
  • 1520-6106
DOI
10.1021/jp070212j
OpenAlex
W2070246893
Cited by
250
References
1
Citations by year
2026: 6 · 2025: 12 · 2024: 18 · 2023: 12 · 2022: 7 · 2021: 9 · 2020: 10 · 2019: 15 · 2018: 24 · 2017: 11 · 2016: 20 · 2015: 9 · 2014: 15 · 2013: 17 · 2012: 19
FWCI
3.70
Type
journal article
Language
en
Open access
closed
Locations
  • The Journal of Physical Chemistry B (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Center for Research Resources (P20RR015588)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Keywords
protein aggregation kinetics, nucleation and growth, protein unfolding, half-life, extent of reaction, aggregate size distribution, nuclear size, kinetic regime, peptide aggregation
MeSH terms
Algorithms, Half-Life, Kinetics, Models, Chemical, Molecular Weight, Protein Conformation, Proteins, Thermodynamics, Models, Statistical, Protein Folding

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