Journal Article

DZNE-2020-03102

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush.

Wegmann, S. (Corresponding author)Extern* ; Medalsy, I. D. ; Mandelkow, E.DZNE* ; Müller, D. J.

2013
National Acad. of Sciences Washington, DC

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Please use a persistent id in citations: doi:10.1073/pnas.1212100110

Abstract: The structure and properties of amyloid-like Tau fibrils accumulating in neurodegenerative diseases have been debated for decades. Although the core of Tau fibrils assembles from short β-strands, the properties of the much longer unstructured Tau domains protruding from the fibril core remain largely obscure. Applying immunogold transmission EM, and force-volume atomic force microscopy (AFM), we imaged human Tau fibrils at high resolution and simultaneously mapped their mechanical and adhesive properties. Tau fibrils showed a ≈ 16-nm-thick fuzzy coat that resembles a two-layered polyelectrolyte brush, which is formed by the unstructured short C-terminal and long N-terminal Tau domains. The mechanical and adhesive properties of the fuzzy coat are modulated by electrolytes and pH, and thus by the cellular environment. These unique properties of the fuzzy coat help in understanding how Tau fibrils disturb cellular interactions and accumulate in neurofibrillary tangles.

Keyword(s): Adhesiveness (MeSH) ; Biomechanical Phenomena (MeSH) ; Electrolytes: chemistry (MeSH) ; Humans (MeSH) ; Hydrogen-Ion Concentration (MeSH) ; Microscopy, Atomic Force (MeSH) ; Microscopy, Immunoelectron (MeSH) ; Models, Molecular (MeSH) ; Protein Interaction Domains and Motifs (MeSH) ; Protein Multimerization (MeSH) ; Recombinant Proteins: chemistry (MeSH) ; Recombinant Proteins: genetics (MeSH) ; Recombinant Proteins: ultrastructure (MeSH) ; tau Proteins: chemistry (MeSH) ; tau Proteins: genetics (MeSH) ; tau Proteins: physiology (MeSH) ; tau Proteins: ultrastructure (MeSH) ; Electrolytes ; MAPT protein, human ; Recombinant Proteins ; tau Proteins

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Contributing Institute(s):

1. Structural Principles of Neurodegeneration (AG (Eckhard) Mandelkow)

Research Program(s):

1. 342 - Disease Mechanisms and Model Systems (POF3-342) (POF3-342)

Appears in the scientific report 2013

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Database coverage:
; BIOSIS Previews ; Clarivate Analytics Master Journal List ; Current Contents - Agriculture, Biology and Environmental Sciences ; Current Contents - Life Sciences ; Ebsco Academic Search ; IF >= 5 ; JCR ; NCBI Molecular Biology Database ; National-Konsortium ; PubMed Central ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Web of Science Core Collection ; Zoological Record

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