Self-assembly of protein amyloids: a competition between amorphous and ordered aggregation.
Protein aggregation in the form of amyloid fibrils has important biological and technological implications. Although the self-assembly process is highly efficient, aggregates not in the fibrillar form would also occur and it is important to include these disordered species when discussing the thermodynamic equilibrium behavior of the system. Here, we initiate such a task by considering a mixture of monomeric proteins and the corresponding aggregates in the disordered form (micelles) and in the fibrillar form (amyloid fibrils). Starting with a model on the respective binding free energies for these species, we calculate their concentrations at thermal equilibrium. We then discuss how the incorporation of the disordered structure furthers our understanding on the various amyloid promoting factors observed empirically, and on the kinetics of fibrilization.
Lee
Chiu Fan
CF
Physics Department, Clarendon Laboratory, Oxford University, Parks Road, Oxford OX1 3PU, United Kingdom. c.lee1@physics.ox.ac.uk
D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D008958:Models, Molecular; D011312:Pressure; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D013696:Temperature; D013816:Thermodynamics
D000682:Amyloid