Steckmann2012 - Amyloid beta-protein fibrillogenesis (kinetics of secondary structure conversion)

Steckmann2012 - Amyloid beta-protein
fibrillogenesis (kinetics of secondary structure conversion)

This model is described in the article:

Kinetics of peptide
secondary structure conversion during amyloid ?-protein
fibrillogenesis.

Steckmann T, Awan Z, Gerstman BS,
Chapagain PP.
J. Theor. Biol. 2012 May; 301:
95-102
Abstract:

Amyloid fibrils are a common component in many debilitating
human neurological diseases such as Alzheimer's (AD),
Parkinson's, and Creutzfeldt-Jakob, and in animal diseases such
as BSE. The role of fibrillar ?? proteins in AD has stimulated
interest in the kinetics of ?? fibril formation. Kinetic models
that include reaction pathways and rate parameters for the
various stages of the process can be helpful towards
understanding the dynamics on a molecular level. Based upon
experimental data, we have developed a mathematical model for
the reaction pathways and determined rate parameters for
peptide secondary structural conversion and aggregation during
the entire fibrillogenesis process from random coil to mature
fibrils, including the molecular species that accelerate the
conversions. The model and the rate parameters include
different molecular structural stages in the nucleation and
polymerization processes and the numerical solutions yield
graphs of concentrations of different molecular species versus
time that are in close agreement with experimental results. The
model also allows for the calculation of the time-dependent
increase in aggregate size. The calculated results agree well
with experimental results, and allow differences in
experimental conditions to be included in the calculations. The
specific steps of the model and the rate constants that are
determined by fitting to experimental data provide insight on
the molecular species involved in the fibril formation
process.

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