The solution structure of the C-terminal segment of tau protein

Gennaro Esposito, P. Viglino, M. Novak, A. Cattaneo

    Research output: Contribution to journalArticle

    Abstract

    Pathological changes in the microtubule associated protein tau, leading to tau-containing filamentous lesions, are a major hallmark common to many types of human neurodegenerative diseases, including Alzheimer's disease (AD). No structural data are available which could rationalize the extensive conformational changes that occur when tau protein is converted to Alzheimer's paired helical filaments (PHF). The C-terminal portion of tau plays a crucial role in the aggregation of tau into PHF and in the truncation process that generates cytotoxic segments of tau. Therefore, we investigated the solution structure of the hydrophobic C-terminal segment 423-441 of tau protein (PQLATLADEVSASLAKQGL) by 1H 2D NMR spectroscopy. The peptide displays the typical NMR evidence consistent with a α-helix geometry with a stabilizing C-capping motif. The reported data represent the first piece of structural information on an important portion of the molecule and can have implications towards the understanding of its pathophysiology. Copyright (C) 2000 European Peptide society and John Wiley and Sons, Ltd.

    Original languageEnglish (US)
    Pages (from-to)550-559
    Number of pages10
    JournalJournal of Peptide Science
    Volume6
    Issue number11
    DOIs
    StatePublished - Dec 28 2000

    Fingerprint

    tau Proteins
    Neurodegenerative diseases
    Peptides
    Microtubule-Associated Proteins
    Neurodegenerative Diseases
    Nuclear magnetic resonance spectroscopy
    Alzheimer Disease
    Magnetic Resonance Spectroscopy
    Agglomeration
    Nuclear magnetic resonance
    Molecules
    Geometry
    Proton Magnetic Resonance Spectroscopy

    Keywords

    • α-helix conformation
    • Alzheimer's disease
    • C-capping
    • Helix capping
    • NMR of peptides
    • NMR structure
    • Protection from proteolysis
    • Tau protein

    ASJC Scopus subject areas

    • Structural Biology
    • Biochemistry
    • Molecular Medicine
    • Molecular Biology
    • Pharmacology
    • Drug Discovery
    • Organic Chemistry

    Cite this

    The solution structure of the C-terminal segment of tau protein. / Esposito, Gennaro; Viglino, P.; Novak, M.; Cattaneo, A.

    In: Journal of Peptide Science, Vol. 6, No. 11, 28.12.2000, p. 550-559.

    Research output: Contribution to journalArticle

    Esposito, Gennaro ; Viglino, P. ; Novak, M. ; Cattaneo, A. / The solution structure of the C-terminal segment of tau protein. In: Journal of Peptide Science. 2000 ; Vol. 6, No. 11. pp. 550-559.
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