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Deriving kinetic parameters of amyloid aggregation from concentration dependence of lag phaseстатья Исследовательская статья
Информация о цитировании статьи получена из
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 23 января 2026 г.
- Авторы: Vasilenko Egor O., Ivankov Dmitry N.
- Журнал: European Physical Journal Plus
- Том: 140
- Номер: 12
- Год издания: 2025
- Номер статьи: 1251
- DOI: 10.1140/epjp/s13360-025-07180-5
- Аннотация: Many peptides and proteins self-assemble into large fibrillar aggregates, reaching sizes of several micrometers. This process typically involves nucleation, formation of transient oligomeric species ranging from dimers to assemblies comprising hundreds of monomers. The roles of these heterogeneous structures in initiating fibril growth vary significantly, as only some convert into primary nuclei, the smallest spontaneously elongating assemblies. The initial stages of peptide aggregation remain a critical challenge in understanding amyloid fibril formation. Here, we analyze the aggregation lag time as a function of initial peptide concentration, employing linear regression on a double-logarithmic scale to derive the critical nucleus size from the slope. We show that selection of linearizing coordinates depends on kinetic regime, and derive appropriate scaling for exponential propagation driven by random fragmentation or erosion. The model also proves that linear and surface growth models cannot capture the weak concentration dependence of lag times for several peptides, and erosion or random fragmentation has to be considered. Inclusion of capping and fragmentation mechanisms substantially improves the plausibility of the model. Although peptide length has no clear correlation with nucleus size, extended helical regions including α- and other helices may promote the formation of larger nuclei,stabilizing preliminary oligomers and prolonging the lag phase. We quantified the contributions of higher-order oligomers as on-and off-pathway species across multiple peptides, identifying a common critical micelle concentration range.
- Добавил в систему: Василенко Егор Олегович