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Updated: Jul 30, 2025

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
Published on: November 30, 2018
Ganglioside GM1 produces stable, short, and cytotoxic Aβ40 protofibrils
Manjeet Kumar1, Magdalena I Ivanova2, Ayyalusamy Ramamoorthy1
1Biophysics, Department of Chemistry, Biomedical Engineering, Macromolecular Science and Engineering, Michigan Neuroscience Institute, University of Michigan, Ann Arbor, MI 48109-1055, USA. ramamoor@umich.edu.
Abstract:
Monosialoganglioside GM1-bound amyloid β-peptides have been found in patients' brains exhibiting early pathological changes of Alzheimer's disease. Herein, we report the ability of non-micellar GM1 to modulate Aβ40 aggregation resulting in the formation of stable, short, rod-like, and cytotoxic Aβ40 protofibrils with the ability to potentiate both Aβ40 and Aβ42 aggregation.
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