Cargando…

Conformation-Specific Association of Prion Protein Amyloid Aggregates with Tau Protein Monomers

Protein aggregation into amyloid fibrils is associated with several amyloidoses, including neurodegenerative Alzheimer’s and Parkinson’s diseases. Despite years of research and numerous studies, the process is still not fully understood, which significantly impedes the search for cures of amyloid-re...

Descripción completa

Detalles Bibliográficos
Autores principales: Ziaunys, Mantas, Mikalauskaite, Kamile, Krasauskas, Lukas, Smirnovas, Vytautas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10253018/
https://www.ncbi.nlm.nih.gov/pubmed/37298227
http://dx.doi.org/10.3390/ijms24119277
_version_ 1785056307853656064
author Ziaunys, Mantas
Mikalauskaite, Kamile
Krasauskas, Lukas
Smirnovas, Vytautas
author_facet Ziaunys, Mantas
Mikalauskaite, Kamile
Krasauskas, Lukas
Smirnovas, Vytautas
author_sort Ziaunys, Mantas
collection PubMed
description Protein aggregation into amyloid fibrils is associated with several amyloidoses, including neurodegenerative Alzheimer’s and Parkinson’s diseases. Despite years of research and numerous studies, the process is still not fully understood, which significantly impedes the search for cures of amyloid-related disorders. Recently, there has been an increase in reports of amyloidogenic protein cross-interactions during the fibril formation process, which further complicates the already intricate process of amyloid aggregation. One of these reports displayed an interaction involving Tau and prion proteins, which prompted a need for further investigation into the matter. In this work, we generated five populations of conformationally distinct prion protein amyloid fibrils and examined their interaction with Tau proteins. We observed that there was a conformation-specific association between Tau monomers and prion protein fibrils, which increased the aggregate self-association and amyloidophilic dye binding capacity. We also determined that the interaction did not induce the formation of Tau protein amyloid aggregates, but rather caused their electrostatic adsorption to the prion protein fibril surface.
format Online
Article
Text
id pubmed-10253018
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-102530182023-06-10 Conformation-Specific Association of Prion Protein Amyloid Aggregates with Tau Protein Monomers Ziaunys, Mantas Mikalauskaite, Kamile Krasauskas, Lukas Smirnovas, Vytautas Int J Mol Sci Article Protein aggregation into amyloid fibrils is associated with several amyloidoses, including neurodegenerative Alzheimer’s and Parkinson’s diseases. Despite years of research and numerous studies, the process is still not fully understood, which significantly impedes the search for cures of amyloid-related disorders. Recently, there has been an increase in reports of amyloidogenic protein cross-interactions during the fibril formation process, which further complicates the already intricate process of amyloid aggregation. One of these reports displayed an interaction involving Tau and prion proteins, which prompted a need for further investigation into the matter. In this work, we generated five populations of conformationally distinct prion protein amyloid fibrils and examined their interaction with Tau proteins. We observed that there was a conformation-specific association between Tau monomers and prion protein fibrils, which increased the aggregate self-association and amyloidophilic dye binding capacity. We also determined that the interaction did not induce the formation of Tau protein amyloid aggregates, but rather caused their electrostatic adsorption to the prion protein fibril surface. MDPI 2023-05-25 /pmc/articles/PMC10253018/ /pubmed/37298227 http://dx.doi.org/10.3390/ijms24119277 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Ziaunys, Mantas
Mikalauskaite, Kamile
Krasauskas, Lukas
Smirnovas, Vytautas
Conformation-Specific Association of Prion Protein Amyloid Aggregates with Tau Protein Monomers
title Conformation-Specific Association of Prion Protein Amyloid Aggregates with Tau Protein Monomers
title_full Conformation-Specific Association of Prion Protein Amyloid Aggregates with Tau Protein Monomers
title_fullStr Conformation-Specific Association of Prion Protein Amyloid Aggregates with Tau Protein Monomers
title_full_unstemmed Conformation-Specific Association of Prion Protein Amyloid Aggregates with Tau Protein Monomers
title_short Conformation-Specific Association of Prion Protein Amyloid Aggregates with Tau Protein Monomers
title_sort conformation-specific association of prion protein amyloid aggregates with tau protein monomers
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10253018/
https://www.ncbi.nlm.nih.gov/pubmed/37298227
http://dx.doi.org/10.3390/ijms24119277
work_keys_str_mv AT ziaunysmantas conformationspecificassociationofprionproteinamyloidaggregateswithtauproteinmonomers
AT mikalauskaitekamile conformationspecificassociationofprionproteinamyloidaggregateswithtauproteinmonomers
AT krasauskaslukas conformationspecificassociationofprionproteinamyloidaggregateswithtauproteinmonomers
AT smirnovasvytautas conformationspecificassociationofprionproteinamyloidaggregateswithtauproteinmonomers