PIP2 Phospholipid-Induced Aggregation of Tau Filaments Probed by Tip-Enhanced Raman Spectroscopy: Angew.Chem.Int

PIP2 Phospholipid-Induced Aggregation of Tau Filaments Probed by Tip-Enhanced Raman Spectroscopy: Angew.Chem.Int

The morphology and secondary structure of peptide fibers formed by aggregation of tubulin-associated unit (Tau) fragments (K18), in the presence of the inner cytoplasmic membrane phosphatidylinositol component (PIP2 ) or heparin sodium (HS) as cofactors, are determined with nanoscale (

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Veröffentlicht in:Angewandte Chemie International Edition 2018, Vol.57 (48), p.15738-15742
Hauptverfasser: Talaga, David, Smeralda, Willy, Lescos, Laurie, Hunel, Julien, Lepejova-Caudy, Nad'A, Cullin, Christophe, Bonhommeau, Sébastien, Lecomte, Sophie
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container_end_page 15742
container_issue 48
container_start_page 15738
container_title Angewandte Chemie International Edition
container_volume 57
creator Talaga, David
Smeralda, Willy
Lescos, Laurie
Hunel, Julien
Lepejova-Caudy, Nad'A
Cullin, Christophe
Bonhommeau, Sébastien
Lecomte, Sophie
description The morphology and secondary structure of peptide fibers formed by aggregation of tubulin-associated unit (Tau) fragments (K18), in the presence of the inner cytoplasmic membrane phosphatidylinositol component (PIP2 ) or heparin sodium (HS) as cofactors, are determined with nanoscale (
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By means of tip-enhanced Raman spectroscopy (TERS), the inclusion of PIP2 lipids in fibers is determined based on the observation of specific C=O ester vibration modes. Moreover, analysis of amide I and amide III bands suggests that the parallel beta-sheet secondary structure content is lower and the random coil content is higher for fibers grown from the PIP2 cofactor instead of HS. These observations highlight the occurrence of some local structural differences between these fibers. 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Material chemistry
title PIP2 Phospholipid-Induced Aggregation of Tau Filaments Probed by Tip-Enhanced Raman Spectroscopy: Angew.Chem.Int
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