Exploring the role of halogen substituents in the ability of a series of fluorescein derivatives to modulate peptide aggregation
Abstract:
Amyloid beta is a relatively small peptide (~40 amino acids) known to aggregate in Alzheimers-associated neurotoxic oligomers via beta-sheet formation. Recent studies have shown that specific halogen substitution of fluorescein can effectively modulate peptide aggregation; the mechanism by which these molecules prevent aggregation and the specific interactions between these derivatives and amyloid beta have not been elucidated. Nuclear magnetic resonance spectroscopy has been used to investigate the details of these interactions, and x-ray absorption spectroscopy (XAS) has been applied to specifically probe the role of the halogen substituent in mediating amyloid beta aggregation.