Amphotericin B interactions with soluble oligomers of amyloid Aβ1-42 peptide

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, β-structure-rich soluble oligomeric forms of Aβ1-42 peptide, yet amphotericin B has no measurable impact neither on the secondary structure nor on time-dependent aggregation profile of the amyloid peptide.

Amphotericin B is a potential spectroscopic probe for a random coil and β-sheet conformations of soluble Aβ1-42 oligomers.Figure optionsDownload as PowerPoint slide