Arginine π-stacking drives binding to fibrils of the Alzheimer protein Tau

Tau fibril formation is a hallmark of Alzheimer’s disease. Here the authors reveal an aggregation-dependent protein interaction pattern of Tau and further show that π-stacking of the arginine side-chains drives aberrant protein binding to Tau fibrils.

Bibliographic Details
Main Authors: Luca Ferrari, Riccardo Stucchi, Katerina Konstantoulea, Gerarda van de Kamp, Renate Kos, Willie J. C. Geerts, Laura S. van Bezouwen, Friedrich G. Förster, Maarten Altelaar, Casper C. Hoogenraad, Stefan G. D. Rüdiger
Format: Article
Language:English
Published: Nature Publishing Group 2020-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-13745-7
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spelling doaj-1e2a4433b35f46b3b264a6a1c10869f92021-05-11T09:20:20ZengNature Publishing GroupNature Communications2041-17232020-01-0111111310.1038/s41467-019-13745-7Arginine π-stacking drives binding to fibrils of the Alzheimer protein TauLuca Ferrari0Riccardo Stucchi1Katerina Konstantoulea2Gerarda van de Kamp3Renate Kos4Willie J. C. Geerts5Laura S. van Bezouwen6Friedrich G. Förster7Maarten Altelaar8Casper C. Hoogenraad9Stefan G. D. Rüdiger10Cellular Protein Chemistry, Bijvoet Center for Biomolecular Research, Utrecht UniversityScience for Life, Utrecht UniversityCellular Protein Chemistry, Bijvoet Center for Biomolecular Research, Utrecht UniversityCellular Protein Chemistry, Bijvoet Center for Biomolecular Research, Utrecht UniversityCellular Protein Chemistry, Bijvoet Center for Biomolecular Research, Utrecht UniversityScience for Life, Utrecht UniversityScience for Life, Utrecht UniversityScience for Life, Utrecht UniversityScience for Life, Utrecht UniversityScience for Life, Utrecht UniversityCellular Protein Chemistry, Bijvoet Center for Biomolecular Research, Utrecht UniversityTau fibril formation is a hallmark of Alzheimer’s disease. Here the authors reveal an aggregation-dependent protein interaction pattern of Tau and further show that π-stacking of the arginine side-chains drives aberrant protein binding to Tau fibrils.https://doi.org/10.1038/s41467-019-13745-7
collection DOAJ
language English
format Article
sources DOAJ
author Luca Ferrari
Riccardo Stucchi
Katerina Konstantoulea
Gerarda van de Kamp
Renate Kos
Willie J. C. Geerts
Laura S. van Bezouwen
Friedrich G. Förster
Maarten Altelaar
Casper C. Hoogenraad
Stefan G. D. Rüdiger
spellingShingle Luca Ferrari
Riccardo Stucchi
Katerina Konstantoulea
Gerarda van de Kamp
Renate Kos
Willie J. C. Geerts
Laura S. van Bezouwen
Friedrich G. Förster
Maarten Altelaar
Casper C. Hoogenraad
Stefan G. D. Rüdiger
Arginine π-stacking drives binding to fibrils of the Alzheimer protein Tau
Nature Communications
author_facet Luca Ferrari
Riccardo Stucchi
Katerina Konstantoulea
Gerarda van de Kamp
Renate Kos
Willie J. C. Geerts
Laura S. van Bezouwen
Friedrich G. Förster
Maarten Altelaar
Casper C. Hoogenraad
Stefan G. D. Rüdiger
author_sort Luca Ferrari
title Arginine π-stacking drives binding to fibrils of the Alzheimer protein Tau
title_short Arginine π-stacking drives binding to fibrils of the Alzheimer protein Tau
title_full Arginine π-stacking drives binding to fibrils of the Alzheimer protein Tau
title_fullStr Arginine π-stacking drives binding to fibrils of the Alzheimer protein Tau
title_full_unstemmed Arginine π-stacking drives binding to fibrils of the Alzheimer protein Tau
title_sort arginine π-stacking drives binding to fibrils of the alzheimer protein tau
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2020-01-01
description Tau fibril formation is a hallmark of Alzheimer’s disease. Here the authors reveal an aggregation-dependent protein interaction pattern of Tau and further show that π-stacking of the arginine side-chains drives aberrant protein binding to Tau fibrils.
url https://doi.org/10.1038/s41467-019-13745-7
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