Amyloid peptide oligomers and fibrils are studied as targets for therapy and diagnosis of Alzheimer’s disease. They are usually detected by amyloid incubation, but such method is necessarily associated with Aβ1–42 depletion and dye binding or conjugation, which have a complex influence on fibril growth, provide information about fibril elongation over long time periods only, and might lead to false-positive results in amyloid inhibition assay. Surface plasmon resonance (SPR) is used to study with no labelling and in real time the aggregation of Aβ1–42 amyloid on specific antibodies. SPR data show, for the first time by using SPR, a multi-phase association behavior for Aβ1–42 oligomers accounting for a sigmoidal growth of amyloid as a function of time, with two antibody-dependent aggregation patterns. The new method represents an advantageous alternative to traditional procedures for investigating amyloid self-assembly and inhibition from early-stage oligomer association, on the time scale of seconds to minutes, to long-term polymerization, on the time scale of hours to days.
|Titolo:||Surface plasmon resonance for the label-free detection of Alzheimer’s β-amyloid peptide aggregation|
|Data di pubblicazione:||2016|
|Citazione:||Surface plasmon resonance for the label-free detection of Alzheimer’s β-amyloid peptide aggregation / Pasquale Palladino; Angela M. Aura; SPOTO G. - In: ANALYTICAL AND BIOANALYTICAL CHEMISTRY. - ISSN 1618-2642. - 408:3(2016), pp. 849-854.|
|Appare nelle tipologie:||1.1 Articolo in rivista|