The extent of protein hydration dictates the preference for heterogeneous or homogeneous nucleation generating either parallel or antiparallel β-sheet α-synuclein aggregates-Reference-Cited by-同舟云学术

The extent of protein hydration dictates the preference for heterogeneous or homogeneous nucleation generating either parallel or antiparallel β-sheet α-synuclein aggregates

Published:2020 Issue:43 Volume:11 Page:11902-11914
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Camino José D.¹²³⁴,Gracia Pablo¹²³⁴^ORCID,Chen Serene W.⁵⁶⁷⁸⁹,Sot Jesús¹⁰¹¹¹²⁴^ORCID,de la Arada Igor¹⁰¹¹¹²⁴^ORCID,Sebastián Víctor¹³¹⁴¹⁵⁴¹⁶^ORCID,Arrondo José L. R.¹⁰¹¹¹²⁴¹⁷,Goñi Félix M.¹⁰¹¹¹²⁴¹⁷^ORCID,Dobson Christopher M.⁵⁶⁷⁸⁹,Cremades Nunilo¹²³⁴

Affiliation:

1. Biocomputation and Complex Systems Physics Institute (BIFI)-Joint Unit BIFI-IQFR (CSIC)

2. University of Zaragoza

3. 50018 Zaragoza

4. Spain

5. Centre for Misfolding Diseases

6. Department of Chemistry

7. University of Cambridge

8. Cambridge CB2 1EW

9. UK

10. Biofisika Institute (CSIC, UPV/EHU)

11. University of the Basque Country

12. 48940 Leioa

13. Instituto de Nanociencia y Materiales de Aragon (INMA)

14. CSIC-Universidad de Zaragoza

15. 50009 Zaragoza

16. Department of Chemical and Enviromental Engineering

17. Department of Biochemistry and Molecular Biology

Abstract

The extent of protein hydration modulates the free energy barrier of both heterogeneous and homogeneous α-synuclein nucleation, leading to the formation of distinct amyloid polymorphs depending on the water activity of the protein microenvironment.

Funder

Eusko Jaurlaritza

European Commission

Ministerio de Economía y Competitividad

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2020/SC/D0SC05297C

Reference82 articles.

1. Filamentous α-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies