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Five peptide fragments [Aβ 17–21 ; Aβ 25–29 ; Aβ 29–33 ; Aβ 33–37 ; Aβ 25–37 ] of the toxic Aβ 1–40(42) amyloid peptide were shown to bind with neuronal nitric oxide synthase by means of hydrophobic–hydrophobic forces. The enzyme has a single site for the amyloid peptide binding, which resulted in a quenching of the intrinsic fluorescence of the enzyme...
Aggregated β-amyloid deposit is a hallmark in the neuropathology of Alzheimer’s disease but their mechanism of formation still remains unresolved. Previously we reported that a normal pentapeptide Aβ 17-21 and glycine zipper peptide Aβ 29-33 strongly inhibited nitric oxide synthase and rapidly initiated fibrillogenesis. Critical amino acids within these fragments were not identified...
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