Effect of Surfaces on Amyloid Fibril Formation

2017/04/26 by Brad Moores, Moores, Brad, Elizabeth Drolle +7
Biochemistry, Genetics and Molecular Biology · Materials Science · Medicine · #Alzheimer's disease research and treatments #Biological Physics (physics.bio-ph) #Biomolecules (q-bio.BM) #FOS: Biological sciences #FOS: Physical sciences #Lipid Membrane Structure and Behavior #Supramolecular Self-Assembly in Materials

paper · pdf · doi:10.48550/arxiv.1704.08319

openalex publication_date 2017/04/26 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28

Abstract

Using atomic force microscopy (AFM) we investigated the interaction of amyloid beta (Ab) (1 42) peptide with chemically modified surfaces in order to better understand the mechanism of amyloid toxicity, which involves interaction of amyloid with cell membrane surfaces. We compared the structure and density of Ab fibrils on positively and negatively charged as well as hydrophobic chemically modified surfaces at physiologically relevant conditions.

Citations

• Protein Misfolding, Functional Amyloid, and Human Disease

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