Affiliations: [a] Centre for Science and Technology in Medicine, Keele University, Staffordshire, UK | [b] School of Biochemistry & Molecular Biology, University of Leeds, Leeds, UK | [c] Department of Inorganic and Analytical Chemistry, University of Szeged, Szeged, Hungary | [d] Birchall Centre for Inorganic Chemistry and Materials Science, Keele University, Staffordshire, UK
Correspondence:
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Corresponding author: Dr. C. Exley, School of Chemistry and Physics, Keele University, Staffordshire, ST5 5BG, UK. Tel.: +44 1782 584080; Fax: +44 1782 712378; E-mail: [email protected].
Abstract: The catabolism of amyloid beta peptides (Aβ) may be important in their accumulation in the brain in both early and late-onset Alzheimer's disease (AD). The serine protease plasmin is one of a suite of proteases implicated in AD. It is a promoter of α-cleavage of the amyloid β precursor protein (AβPP) and will degrade Aβ in vitro. Herein we have demonstrated cleavage of the amyloidogenic Aβ25–35 by plasmin to produce the non-amyloidogenic fragment Aβ25–35. The activity of plasmin was halved by pre-mixing it with aluminium (Al) prior to its addition to the peptide. An interaction between Al and proteases involved in the catabolism of Aβ might define the putative link between Al and AD.
