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Amyloids and Micelles : Self-assembly and co-assembly of Abeta and gangliosides

In English

Författare

Summary, in English

Extracellular plaques in Alzheimer’s disease contain Aβ peptides and ganglioside lipids such as GM1. Aβ monomers self-assemble into beta-sheet-rich fibrils when their concentration exceeds solubility, while GM1 monomers form spherical micelles above their critical concentration. This study examines the self-assembly of Aβ in the first two papers and its co-assembly with GM1 in the last two. In Paper I, we investigate whether the secondary nucleation sites of Aβ are defects on fibrils, using the secondary nucleation sites binding chaperone–Brichos. We found that secondary nucleation sites are rare and that fibrils formed under low supersaturation exhibit fewer secondary nucleation sites than those formed under high supersaturation. In Paper II, we examine the impact of shear force from mild agitation on Aβ kinetics. Our findings show that mild agitation accelerates both primary and secondary nucleation, particularly the detachment step of the latter. Papers III and IV explore the co-assembly of Aβ and GM1 and its effects on Aβ aggregation kinetics and thermodynamics. We found that Aβ and GM1 form micellar co-assemblies, with Aβ evenly distributed among co-assemblies, likely positioned at the interface between GM1’s hydrophobic chains and head groups. This co-assembly reduces both the aggregation speed and solubility of Aβ.

Publiceringsår

2024

Språk

Engelska

Dokumenttyp

Doktorsavhandling

Förlag

Lund University

Ämne

  • Physical Chemistry (including Surface- and Colloid Chemistry)

Nyckelord

  • Amyloid Beta
  • ganglioside lipids
  • kinetic
  • thermodynamic

Aktiv

Published

ISBN/ISSN/Övrigt

  • ISBN: 978-91-8096-088-5
  • ISBN: 978-91-8096-089-2

Försvarsdatum

31 januari 2025

Försvarstid

09:00

Försvarsplats

KC:A. Join via zoom: https://lu-se.zoom.us/j/61647037626

Opponent

  • Christofer Lendel (Associate professor)