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Updated: Jun 25, 2026

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
Published on: May 22, 2018
Amphotericin B interactions with soluble oligomers of amyloid Abeta1-42 peptide
Nicholas W Smith1, Onofrio Annunziata, Sergei V Dzyuba
1Department of Chemistry, Texas Christian University, Fort Worth, TX 76129, USA.
Abstract:
Amphotericin B has recently been suggested as an efficient inhibitor of amyloid peptide fibril formation; however its interactions with more neurotoxic, soluble forms of amyloid peptides have not been reported to date. Circular dichroism spectroscopy allowed for distinguishing between the binding and inhibition of aggregation events: amphotericin B distinctly interacts with both unordered and ordered, beta-structure-rich soluble oligomeric forms of Abeta1-42 peptide, yet amphotericin B has no measurable impact neither on the secondary structure nor on time-dependent aggregation profile of the amyloid peptide.
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