Kinetic studies of inhibition of the amyloid beta (1-42) aggregation using a ferrocene-tagged β-sheet breaker peptide.

ABSTRACT: The aggregation of amyloidogenic proteins/peptides has been closely linked to the neuropathology of several important neurological disorders. In Alzheimer's disease, amyloid beta (Aβ) peptides and their aggregation are believed to be at least partially responsible for the etiology of Alzheimer's disease. The aggregate-inflicted cellular toxicity can be inhibited by short peptides whose sequences are homologous to segments of the Aβ(1-42) peptide responsible for β-sheet stacking (referred to as the β-sheet breaker peptides). Here, a water-soluble ferrocene (Fc)-tagged β-sheet breaker peptide, Fc-KLVFFK(6), was used as an electrochemical probe for kinetic studies of the inhibition of the Aβ(1-42) fibrillation process and for determination of the optimal concentration of β-sheet breaker pepti

SUBMITTER: Zhang L 

PROVIDER: S-EPMC3565064 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature