2008/02/29 by Chiu Fan Lee
Agricultural and Biological Sciences · Biochemistry, Genetics and Molecular Biology · Medicine · Physics and Astronomy · #Alzheimer's disease research and treatments #Protein Structure and Dynamics #Proteins in Food Systems #cond-mat.soft #physics.bio-ph #q-bio.BM
paper · pdf · doi:10.1103/physreve.80.031922
published as Physical Review E 80, 031922 (2009) · Minor changes in the presentation
arxiv created 2009/08/12 · openalex publication_date 2009/09/30 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
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.