Thermodynamic characterization of amyloid polymorphism by microfluidic transient incomplete separation-Reference-Cited by-同舟云学术

Thermodynamic characterization of amyloid polymorphism by microfluidic transient incomplete separation

Published:2024 Issue:7 Volume:15 Page:2528-2544
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Farzadfard Azad¹²^ORCID,Kunka Antonin¹^ORCID,Mason Thomas Oliver¹,Larsen Jacob Aunstrup¹^ORCID,Norrild Rasmus Krogh¹^ORCID,Dominguez Elisa Torrescasana¹,Ray Soumik¹^ORCID,Buell Alexander K.¹^ORCID

Affiliation:

1. Protein Biophysics Group, Department of Biotechnology and Biomedicine, Technical University of Denmark, Søltofts Plads, Building 227, Kgs. Lyngby, 2800, Denmark

2. Interdisciplinary Nanoscience Center (iNANO), Aarhus University, Gustav Wieds Vej 14, 8000, Aarhus C, Denmark

Abstract

Amyloid fibrils of α-synuclein are a hallmark of Parkinsons disease and in this study, we characterise the thermodynamic stability of different amyloid polymorphs.

Funder

HORIZON EUROPE European Research Council

HORIZON EUROPE Marie Sklodowska-Curie Actions

Lundbeck Foundation

Michael J. Fox Foundation for Parkinson's Research

Novo Nordisk Fonden

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/SC/D3SC05371G

Reference90 articles.

1. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade