TY - JOUR
T1 - Thermodynamic properties of amyloid fibrils
T2 - A simple model of peptide aggregation
AU - Urbic, Tomaz
AU - Dias, Cristiano L.
N1 - Funding Information:
T. U. are grateful for the support of the NIH ( GM063592 ) and Slovenian Research Agency ( P1 0103-0201, N1-0042 ) and the National Research, Development and Innovation Office of Hungary ( SNN 116198 ).
Funding Information:
T. U. are grateful for the support of the NIH (GM063592) and Slovenian Research Agency (P1 0103-0201, N1-0042) and the National Research, Development and Innovation Office of Hungary (SNN 116198).
Publisher Copyright:
© 2019 Elsevier B.V.
PY - 2019/6/15
Y1 - 2019/6/15
N2 - In this manuscript, we develop a two-dimensional coarse-grained model to study equilibrium properties of fibril-like structures made of amyloid proteins. The phase space of the model is sampled using Monte Carlo computer simulations. At low densities and high temperatures proteins are mostly present as monomers while at low temperatures and high densities particles self-assemble into fibril-like structures. The phase space of the model is explored and divided into different regions based on the structures present. We also estimate free-energies to dissociate proteins from fibrils based on the residual concentration of dissolved proteins. Consistent with experiments, the concentration of proteins in solution does not affects their equilibrium state. Also, we study the temperature dependence of the equilibrium state to estimate thermodynamic quantities, e.g., heat capacity and entropy, of amyloid fibrils.
AB - In this manuscript, we develop a two-dimensional coarse-grained model to study equilibrium properties of fibril-like structures made of amyloid proteins. The phase space of the model is sampled using Monte Carlo computer simulations. At low densities and high temperatures proteins are mostly present as monomers while at low temperatures and high densities particles self-assemble into fibril-like structures. The phase space of the model is explored and divided into different regions based on the structures present. We also estimate free-energies to dissociate proteins from fibrils based on the residual concentration of dissolved proteins. Consistent with experiments, the concentration of proteins in solution does not affects their equilibrium state. Also, we study the temperature dependence of the equilibrium state to estimate thermodynamic quantities, e.g., heat capacity and entropy, of amyloid fibrils.
KW - Aggregation
KW - Fibrils
KW - Monte Carlo
UR - http://www.scopus.com/inward/record.url?scp=85062150346&partnerID=8YFLogxK
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U2 - 10.1016/j.fluid.2019.02.002
DO - 10.1016/j.fluid.2019.02.002
M3 - Article
AN - SCOPUS:85062150346
SN - 0378-3812
VL - 489
SP - 104
EP - 110
JO - Fluid Phase Equilibria
JF - Fluid Phase Equilibria
ER -