Serum Amyloid P Component Accelerates the Formation and Enhances the Stability of Amyloid Fibrils in a Physiologically Significant Under-Saturated Solution of Amyloid-β₄₂

Article type: Research Article

Authors: Mold, Matthew^{a; b} | Shrive, Annette K.^b | Exley, Christopher^{a; *}

Affiliations: [a] The Birchall Centre, Lennard-Jones Laboratories, Keele University, Staffordshire, UK | [b] Institute of Science and Technology in Medicine, School of Life Sciences, Keele University, Staffordshire, UK

Correspondence: [*] Correspondence to: Dr C. Exley, The Birchall Centre, Lennard-Jones Laboratories, Keele University, Staffordshire, ST5 5BG, UK. E-mail: c.exley@chem.keele.ac.uk.

Abstract: The mechanism whereby an under-saturated solution of amyloid-β (Aβ)42 precipitates as β sheets in vivo in Alzheimer's disease remains to be elucidated. Herein we present in vitro evidence that serum amyloid P component may mediate this process through its acceleration of amyloid formation from an under-saturated solution of Aβ42 and subsequently its stabilization of the amyloid fibrils formed over physiologically significant timeframes. Our observations support serum amyloid P component as a therapeutic target in Alzheimer's disease.

Keywords: Aluminum, amyloid-β, amyloid fibrils, copper, serum amyloid P component, transmission electron microscopy

DOI: 10.3233/JAD-2012-120076

Journal: Journal of Alzheimer's Disease, vol. 29, no. 4, pp. 875-881, 2012