Shardlow, E, Khan, B and Exley, C (2021) Monitoring the early aggregatory behaviour and size of Aβ1-42 in the absence & presence of metal ions using dynamic light scattering. Journal of Trace Elements in Medicine and Biology, 67 (126766). 1- 9. ISSN 0946-672X

[thumbnail of Shardlow 2021 - Abeta1-42 aggregation (full text).pdf] Text
Shardlow 2021 - Abeta1-42 aggregation (full text).pdf - Published Version
Restricted to Repository staff only

Download (3MB)


BACKGROUND AND AIM: Aβ1-42 is an amyloidogenic peptide found within senile plaques extracted from those who died with a diagnosis of Alzheimer's disease. The potent neurotoxicity of this peptide is related to its propensity to form aggregated conformations in vivo, a process that is influenced by the species and concentration of metal ions present within the local environment. This study examines the impact of different metals upon the early aggregatory behaviour and size of Aβ1-42 under simulated physiological conditions. METHODS: The size and aggregatory behaviour of Aβ1-42 in the presence and absence of metal ions was monitored during the initial 30 min of fibril formation in real-time using dynamic light scattering. RESULTS: Intensity scattering measurements showed a clear tendency towards aggregation with regards to Aβ1-42 only solutions (10 μM). Both equimolar Al3+ & Cu2+ lowered and stabilised the dimensions of Aβ1-42 aggregates; however, a diminutive but significant increase in size was still observed over a 30-min period. While excess Al3+ continued to supress the size of Aβ1-42, a 10-fold increase in the concentration of Cu2+ accelerated peptide aggregation relative to that observed for equimolar metal but not compared to Aβ1-42 alone. CONCLUSION: These results infer that Al3+ ions stabilise and aid in the maintenance of smaller, toxic intermediates while excess Cu2+ facilitates the formation of larger, more inert, amorphous species exceeding 1 μm in size. Furthermore, we propose that metal-induced toxicity of Aβ1-42 is reflective of their ability to preserve smaller oligomeric species in vitro.

Item Type: Article
Additional Information: The final version of this article and all relevant information related to it, including copyrights, can be found online at;
Subjects: Q Science > Q Science (General)
Q Science > QD Chemistry
Divisions: Faculty of Natural Sciences > School of Life Sciences
Related URLs:
Depositing User: Symplectic
Date Deposited: 15 Oct 2021 11:00
Last Modified: 15 Oct 2021 11:00

Actions (login required)

View Item
View Item