Thermodynamic properties of amyloid fibrils in equilibrium.
In this manuscript we use a two-dimensional coarse-grained model to study how amyloid fibrils grow towards an equilibrium state where they coexist with proteins dissolved in a solution. Free-energies to dissociate proteins from fibrils are estimated from the residual concentration of dissolved proteins. Consistent with experiments, the concentration of proteins in solution affects the growth rate of fibrils but not their equilibrium state. Also, studies of the temperature dependence of the equilibrium state can be used to estimate thermodynamic quantities, e.g., heat capacity and entropy.
Faculty of Chemistry and Chemical Technology, University of Ljubljana, Vecna pot 113, 1000, Slovenia. Electronic address: tomaz.urbic@fkkt.uni-lj.si.
Tomaz
T
Urbic
National Center for Remote Sensing, National Council for Scientific Research (CNRS), Riad al Soloh, 1107 2260 Beirut, Lebanon.
Sara
S
Najem
New Jersey Institute of Technology, Physics Department, Newark,NJ 07042-1982,United States.
Cristiano L
CL
Dias
D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism; D006860:Hydrogen Bonding; D009010:Monte Carlo Method; D013696:Temperature; D013816:Thermodynamics
D016229:Amyloid beta-Peptides