Self-assembly of protein amyloid: a competition between amorphous and ordered aggregation

Abstract

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.

Minor changes in the presentation

References in corpus (2)

• Thermodynamics of beta-amyloid fibril formation
• Isotropic-nematic phase transition in amyloid fibrilization

Cited by in corpus (9)

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• Elongation dynamics of amyloid fibrils: a rugged energy landscape picture
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• Amyloid Fibril Solubility
• A simplified exactly solvable model for beta-amyloid aggregation
• Statistical Mechanics and Kinetics of Amyloid Fibrillation
• Statistical Mechanical Treatments of Protein Amyloid Formation
• Length distribution of stiff, self-assembled polymers at thermal equilibrium