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Amphotericin B interactions with soluble oligomers of amyloid Ab1-42 peptide Nicholas W. Smith, Onofrio Annunziata, Sergei V. Dzyuba *
 

Summary: Amphotericin B interactions with soluble oligomers of amyloid Ab1-42 peptide
Nicholas W. Smith, Onofrio Annunziata, Sergei V. Dzyuba *
Department of Chemistry, Texas Christian University, Fort Worth, TX 76129, USA
a r t i c l e i n f o
Article history:
Received 22 November 2008
Revised 3 February 2009
Accepted 7 February 2009
Available online 14 February 2009
Keywords:
Alzheimer's disease
Amyloid aggregation
Circular dichroism spectroscopy
Macrolide antibiotic
Natural product
a b s t r a c t
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, b-structure-

  

Source: Annunziata, Onofrio - Department of Chemistry, Texas Christian University

 

Collections: Chemistry