Version 1
: Received: 12 July 2023 / Approved: 13 July 2023 / Online: 13 July 2023 (04:52:16 CEST)
How to cite:
Baker, L.; Kataky, R.; Howes, M.R.; Chazot, P.L. Electrochemical Investigations of Aloysia citrodora Paláu L. Water Extract for Iron-Chelation Abilities in Alzheimer’s Disease. Preprints2023, 2023070878. https://doi.org/10.20944/preprints202307.0878.v1
Baker, L.; Kataky, R.; Howes, M.R.; Chazot, P.L. Electrochemical Investigations of Aloysia citrodora Paláu L. Water Extract for Iron-Chelation Abilities in Alzheimer’s Disease. Preprints 2023, 2023070878. https://doi.org/10.20944/preprints202307.0878.v1
Baker, L.; Kataky, R.; Howes, M.R.; Chazot, P.L. Electrochemical Investigations of Aloysia citrodora Paláu L. Water Extract for Iron-Chelation Abilities in Alzheimer’s Disease. Preprints2023, 2023070878. https://doi.org/10.20944/preprints202307.0878.v1
APA Style
Baker, L., Kataky, R., Howes, M.R., & Chazot, P.L. (2023). Electrochemical Investigations of <em>Aloysia citrodora</em> Paláu L. Water Extract for Iron-Chelation Abilities in Alzheimer’s Disease. Preprints. https://doi.org/10.20944/preprints202307.0878.v1
Chicago/Turabian Style
Baker, L., Melanie-Jayne R. Howes and Paul L. Chazot. 2023 "Electrochemical Investigations of <em>Aloysia citrodora</em> Paláu L. Water Extract for Iron-Chelation Abilities in Alzheimer’s Disease" Preprints. https://doi.org/10.20944/preprints202307.0878.v1
Abstract
Alzheimer’s disease (AD) is the leading cause of dementia, characterised by beta-amyloid plaques, neurofibrillary tangles, and oxidative stress. Iron is suspected to enhance disease progression, and chelation may be a potential treatment. We propose that Aloysia citrodora Paláu (AC), a plant in the Verbenaceae family, can act as a moderate chelator of iron. It may reduce the effect of iron on beta-amyloid 1-42 (Aβ1-42) aggregation. Cyclic voltammetry (CV) and differential pulse voltammetry (DPV) were used to demonstrate that AC can interact with iron (II) and iron (III), the two most abundant forms of iron within the body. DPV was also used to characterise Aβ1-42 aggregation, and two main features were obtained. The first is the tyrosine peak (~0.6 V) decreased in magnitude over time, which is a sign of aggregation and folding. The other is a conglomerate of peaks at ~0 V, whose identity is unknown. Furthermore, iron (II) increased the rate of tyrosine peak depreciation, and the addition of AC negated this induced effect. This implied that iron (II) increases Aβ1-42 aggregation into higher order, and AC may be an effective countermeasure.
Medicine and Pharmacology, Neuroscience and Neurology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
