2009/12/10 by Tuomas P. J. Knowles, Christopher A. Waudby, Glyn L. Devlin +6 · 1 citation
Medicine · Biochemistry, Genetics and Molecular Biology · Materials Science · #Alzheimer's disease research and treatments #Prion Diseases and Protein Misfolding #Supramolecular Self-Assembly in Materials
paper · doi:10.1126/science.1178250
openalex publication_date 2009/12/10 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/31
We present an analytical treatment of a set of coupled kinetic equations that governs the self-assembly of filamentous molecular structures. Application to the case of protein aggregation demonstrates that the kinetics of amyloid growth can often be dominated by secondary rather than by primary nucleation events. Our results further reveal a range of general features of the growth kinetics of fragmenting filamentous structures, including the existence of generic scaling laws that provide mechanistic information in contexts ranging from in vitro amyloid growth to the in vivo development of mammalian prion diseases.