Heavy Metal Ions Binding to Beta-Amyloid and Anti-Amyloid Peptides

Ion Laura
Alexandru Ioan Cuza University of Iasi, VAT 4701126

Abstract

Neurodegenerative diseases are a group of pathologies that mainly affect human brain neurons. Particularly, Alzheimer disease (AD) pathological hallmarks consist in extracellular senile plaque formation due to the accumulation of amyloid β (Aβ), abnormal aggregation of tau protein and oxidation of Aβ peptides in the presence of metal ions. Although metal ions are involved in many biological and biomedical processes, several studies suggest that copper, nickel, aluminum, etc. are also involved in the neurotoxicity of Aβ peptides, by forming peptide-metal complexes. Besides the high interest in studying the aggregation and oligomerization process, recent studies also reference the study of some peptides with neuroprotective action, such as NAP (derived from activity-dependent neuroprotective protein) and its interaction with metal ions. However, there are still some unanswered questions regarding metal ion binding mechanism to Aβ and NAP peptides, and the capability of NAP peptide to inhibit the aggregation process. Here, we studied the interaction of copper, aluminum and nickel with Aβ1-16 and NAP modified peptides. For this purpose, techniques such as: mass spectrometry, atomic force microscopy, fourier-transformation infrared spectroscopy were used to study the metal ions-peptides interaction for a better understanding of metal ions bindings in AD. Our results suggest that the binding of metal ions to peptides is closely linked to the peptide sequence and to the type of metal ion used. Acknowledgements This work was co-funded by the European Social Fund, through Operational Programme Human Capital 2014-2020, project number POCU/380/6/13/123623 (PhD Students and Postdoctoral Researchers Prepared for the Labour Market).


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