Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10154512 | Journal of Trace Elements in Medicine and Biology | 2019 | 8 Pages |
Abstract
Islet amyloid polypeptide (IAPP1-37) or amylin is implicated in the aetiology of diabetes. It is found as amyloid along with its precursor ProIAPP1-48 in the islets of Langerhans in the pancreas. Metals have been implicated in amyloidogenesis of both IAPP and ProIAPP. Herein we have used dynamic light scattering (DLS) to investigate how Al(III) and Cu(II) influence aggregation of ProIAPP1-48 under near-physiological conditions and in a biologically-relevant timeframe. ProIAPP1-48 formed primarily sub-micron particles within 5âmin (e.g. 470ânm at 15μM peptide) that grew to micron-sized particles (1310ânm) within a 30âmin timeframe. Equimolar Al(III) had little influence upon particle size at either 5 (656ânm) or 30âmin (1250ânm) while Cu(II) tended to increase particle size over the same time period (731-1300ânm). It is suggested that any effects of Al(III) and Cu(II) reflected their well known tendencies to support β-sheet or amorphous aggregates of ProIAPP1-48 respectively.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Emma Shardlow, Cassandra Rao, Roman Sattarov, Ling Wu, Paul E. Fraser, Christopher Exley,