Literature DB >> 35546203

Amyloid fibril length distribution from dynamic light scattering data.

Petr A Sokolov1, Valeriy I Rolich2, Olga S Vezo2, Mikhail V Belousov3,4, Stanislav A Bondarev3, Galina A Zhouravleva3, Nina A Kasyanenko2.   

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.
© 2022. European Biophysical Societies' Association.

Entities:  

Keywords:  Amyloid; DLS; EPJE-D-21–00,098; Number distribution; Prion; SEM

Mesh：

Substances：

Year:  2022        PMID： 35546203     DOI： 10.1007/s00249-022-01600-5

Source DB:  PubMed          Journal:  Eur Biophys J        ISSN： 0175-7571            Impact factor:   1.733


  14 in total

1.  Building hydrodynamic bead-shell models for rigid bioparticles of arbitrary shape.

Authors:  J Garcia de la Torre
Journal:  Biophys Chem       Date:  2001-12-25       Impact factor: 2.352

2.  Direct determination of the number-weighted mean radius and polydispersity from dynamic light-scattering data.

Authors:  Philipus J Patty; Barbara J Frisken
Journal:  Appl Opt       Date:  2006-04-01       Impact factor: 1.980

3.  Measurement of amyloid fibril mass-per-length by tilted-beam transmission electron microscopy.

Authors:  Bo Chen; Kent R Thurber; Frank Shewmaker; Reed B Wickner; Robert Tycko
Journal:  Proc Natl Acad Sci U S A       Date:  2009-08-11       Impact factor: 11.205

4.  Physical properties of polymorphic yeast prion amyloid fibers.

Authors:  Carlos E Castro; Jijun Dong; Mary C Boyce; Susan Lindquist; Matthew J Lang
Journal:  Biophys J       Date:  2011-07-20       Impact factor: 4.033

5.  Refractive indices of the collagen fibrils and extrafibrillar material of the corneal stroma.

Authors:  D W Leonard; K M Meek
Journal:  Biophys J       Date:  1997-03       Impact factor: 4.033

6.  Monitoring protein aggregation kinetics with simultaneous multiple sample light scattering.

Authors:  Michael F Drenski; Mark L Brader; Roy W Alston; Wayne F Reed
Journal:  Anal Biochem       Date:  2013-03-07       Impact factor: 3.365

7.  In Sup35p filaments (the [PSI+] prion), the globular C-terminal domains are widely offset from the amyloid fibril backbone.

Authors:  Ulrich Baxa; Paul W Keller; Naiqian Cheng; Joseph S Wall; Alasdair C Steven
Journal:  Mol Microbiol       Date:  2010-12-07       Impact factor: 3.501

8.  Salt-induced modulation of the pathway of amyloid fibril formation by the mouse prion protein.

Authors:  Shweta Jain; Jayant B Udgaonkar
Journal:  Biochemistry       Date:  2010-09-07       Impact factor: 3.162

9.  Effect of charged residues in the N-domain of Sup35 protein on prion [PSI+] stability and propagation.

Authors:  Stanislav A Bondarev; Vadim V Shchepachev; Andrey V Kajava; Galina A Zhouravleva
Journal:  J Biol Chem       Date:  2013-08-21       Impact factor: 5.157

10.  Design of a New [PSI +]-No-More Mutation in SUP35 With Strong Inhibitory Effect on the [PSI +] Prion Propagation.

Authors:  Lavrentii G Danilov; Andrew G Matveenko; Varvara E Ryzhkova; Mikhail V Belousov; Olga I Poleshchuk; Daria V Likholetova; Petr A Sokolov; Nina A Kasyanenko; Andrey V Kajava; Galina A Zhouravleva; Stanislav A Bondarev
Journal:  Front Mol Neurosci       Date:  2019-11-19       Impact factor: 5.639
View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.