The study of the aggregation of amyloid proteins is challenging. A new approach to processing dynamic light scattering data was developed and tested using aggregates of the well-known model Sup35NM amyloid. After filtering and calculating the moving averages of autocorrelation functions to reduce impacts of noise, each averaged autocorrelation function is converted to the fibril length distribution via numerical modeling. The processing results were verified using atomic force and scanning electron microscopy data. Analysis of fibril length distribution changes over time gives valuable information about the aggregation process.
Translated title of the contributionРаспределение длин амилоидных фибрилл по данным динамического светорассеяния
Original languageEnglish
Pages (from-to)325-333
Number of pages9
JournalEuropean Biophysics Journal
Issue number4-5
Early online date11 May 2022
StatePublished - Jul 2022

    Scopus subject areas

  • Biophysics

    Research areas

  • Amyloid, DLS, EPJE-D-21–00,098, Number distribution, Prion, SEM, 00, EPJE-D-21–00,098,Amyloid,Prion,DLS,Number distribu, dls, 098, number distribution, amyloid, epje-d-21, prion, sem

ID: 95275178