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Amyloid fibril length distribution from dynamic light scattering data. / Соколов, Петр Александрович; Ролич, Валерий Иванович; Везо, Ольга Сергеевна; Белоусов, Михаил Владимирович; Бондарев, Станислав Александрович; Журавлева, Галина Анатольевна; Касьяненко, Нина Анатольевна.

In: European Biophysics Journal, Vol. 51, No. 4-5, 07.2022, p. 325-333.

Research output: Contribution to journal › Article › peer-review

Harvard

Соколов, ПА, Ролич, ВИ, Везо, ОС, Белоусов, МВ, Бондарев, СА, Журавлева, ГА & Касьяненко, НА 2022, 'Amyloid fibril length distribution from dynamic light scattering data', European Biophysics Journal, vol. 51, no. 4-5, pp. 325-333. https://doi.org/10.1007/s00249-022-01600-5

APA

Соколов, П. А., Ролич, В. И., Везо, О. С., Белоусов, М. В., Бондарев, С. А., Журавлева, Г. А., & Касьяненко, Н. А. (2022). Amyloid fibril length distribution from dynamic light scattering data. European Biophysics Journal, 51(4-5), 325-333. https://doi.org/10.1007/s00249-022-01600-5

Vancouver

Соколов ПА, Ролич ВИ, Везо ОС, Белоусов МВ, Бондарев СА, Журавлева ГА et al. Amyloid fibril length distribution from dynamic light scattering data. European Biophysics Journal. 2022 Jul;51(4-5):325-333. https://doi.org/10.1007/s00249-022-01600-5

Author

Соколов, Петр Александрович ; Ролич, Валерий Иванович ; Везо, Ольга Сергеевна ; Белоусов, Михаил Владимирович ; Бондарев, Станислав Александрович ; Журавлева, Галина Анатольевна ; Касьяненко, Нина Анатольевна. / Amyloid fibril length distribution from dynamic light scattering data. In: European Biophysics Journal. 2022 ; Vol. 51, No. 4-5. pp. 325-333.

BibTeX

@article{43465d9723a041d9a017aaeb2fdd9ca1,
title = "Amyloid fibril length distribution from dynamic light scattering data",
abstract = "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.",
keywords = "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",
author = "Соколов, {Петр Александрович} and Ролич, {Валерий Иванович} and Везо, {Ольга Сергеевна} and Белоусов, {Михаил Владимирович} and Бондарев, {Станислав Александрович} and Журавлева, {Галина Анатольевна} and Касьяненко, {Нина Анатольевна}",
note = "Publisher Copyright: {\textcopyright} 2022, European Biophysical Societies' Association.",
year = "2022",
month = jul,
doi = "10.1007/s00249-022-01600-5",
language = "English",
volume = "51",
pages = "325--333",
journal = "European Biophysics Journal",
issn = "0175-7571",
publisher = "Springer Nature",
number = "4-5",

}

RIS

TY - JOUR

T1 - Amyloid fibril length distribution from dynamic light scattering data

AU - Соколов, Петр Александрович

AU - Ролич, Валерий Иванович

AU - Везо, Ольга Сергеевна

AU - Белоусов, Михаил Владимирович

AU - Бондарев, Станислав Александрович

AU - Журавлева, Галина Анатольевна

AU - Касьяненко, Нина Анатольевна

N1 - Publisher Copyright: © 2022, European Biophysical Societies' Association.

PY - 2022/7

Y1 - 2022/7

N2 - 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.

AB - 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.

KW - Amyloid

KW - DLS

KW - EPJE-D-21–00,098

KW - Number distribution

KW - Prion

KW - SEM

KW - 00

KW - EPJE-D-21–00,098,Amyloid,Prion,DLS,Number distribu

KW - dls

KW - 098

KW - number distribution

KW - amyloid

KW - epje-d-21

KW - prion

KW - sem

UR - https://link.springer.com/article/10.1007/s00249-022-01600-5

UR - http://www.scopus.com/inward/record.url?scp=85129877048&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/f1560223-a9e9-369b-bbfd-aee6b956d50e/

U2 - 10.1007/s00249-022-01600-5

DO - 10.1007/s00249-022-01600-5

M3 - Article

VL - 51

SP - 325

EP - 333

JO - European Biophysics Journal

JF - European Biophysics Journal

SN - 0175-7571

IS - 4-5

ER -

ID: 95275178