title: Amphotericin B interactions with soluble oligomers of amyloid Abeta1-42 peptide.
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.
authors.affiliation: Department of Chemistry, Texas Christian University, Fort Worth, TX 76129, USA.
authors.forename: Nicholas W
authors.initials: NW
authors.lastname: Smith
authors.forename: Onofrio
authors.initials: O
authors.lastname: Annunziata
authors.forename: Sergei V
authors.initials: SV
authors.lastname: Dzyuba
mesh_terms: D000666:Amphotericin B / Q000737:chemistry*; D016229:Amyloid beta-Peptides / Q000737:chemistry*; D001704:Biopolymers / Q000737:chemistry*; D002942:Circular Dichroism; D010446:Peptide Fragments / Q000737:chemistry*; D012995:Solubility
chemical_list: D016229:Amyloid beta-Peptides; D001704:Biopolymers; D010446:Peptide Fragments; C075222:amyloid beta-protein (1-42); D000666:Amphotericin B