Peptides of Presenilin-1 Bind the Amyloid Precursor Protein Ectodomain and Offer a Novel and Specific Therapeutic Approach to Reduce β-Amyloid in Alzheimer's Disease


Dewji N, et al., 10(4):e0122451, PLoS One, 2015

Accumulation of β-Amyloid (Aβ) in the brain is believed to be the initiator of Alzheimer's disease (AD). This study demonstrates that two independent peptides, P4 and P8 from within the amino-terminal domain of Presenilin-1 (PS-1) exhibit reduced β-Amyloid (Aβ) production in vitro and also in vivo in the brains of β-amyloid precursor protein (APP) transgenic mice. Bio-Layer Interferometry determined the binding affinities of peptides (P1, scrambled P1, P4, P5, P7, and P8) and APP. A Pall ForteBio Octet RED96 instrument equipped with Streptavidin (SA) biosensors allows capture of biotinylated peptides. The kinetic parameters such as the association rate constant (kon), dissociation rate constant (koff), and binding affinity, KD, were determined. Overall results indicate peptides P4 and P8 have the potential to become drug candidates for the development of successful Alzheimer's disease-modifying therapies.

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