Metalloenzymes for the Potent Treatment of Alzheimer’s Disease and Parkinson’s Disease: A Review

Kim, Namdoo and Lee, Hyuck Jin (2022) Metalloenzymes for the Potent Treatment of Alzheimer’s Disease and Parkinson’s Disease: A Review. In: Progress in Chemical Science Research Vol. 3. B P International, pp. 86-113. ISBN 978-93-5547-776-7

Full text not available from this repository.

Abstract

There has been speculation that a number of amyloidogenic proteins play a role in the onset and progression of neurodegenerative diseases (ND), including Parkinson's disease and Alzheimer's disease (PD). Numerous small compounds have been created to control the aggregation processes of these amyloid proteins in attempt to treat the disorders. In addition to controlling the aggregation of amyloidogenic protiens, maintaining the levels of the proteins in the brain by amyloid degrading enzymes [ADE; neprilysin (NEP), insulin degrading enzyme (IDE), asparagine endopeptidase (AEP), and ADAM10] is essential to cure AD and PD. Therefore, numerous biological molecules and chemical agents have been examined if they could act as inducers or inhibitors against the levels and activities of ADE. Although the removal of amyloidogenic proteins by increasing the activity of ADE may have the unintended consequence side effects, it may result in a relatively good strategy for treating AD and PD. Furthermore, since the causes of ND are diverse, a number of multi-functional (multi-target) chemical agents have been developed to control the actions of multiple ND risk factors, such as amyloidogenic proteins, metal ions, and reactive oxygen species. However, many of them were developed without taking into account how to control ADE levels and behaviours. A possible approach to treating AD and PD would involve combining previously produced compounds with pharmaceutical treatments that treat ADE. In this chapter, the ADE and compounds that can control the activity and expression of the ADE are introduced.

Item Type: Book Section
Subjects: Asian STM > Chemical Science
Depositing User: Managing Editor
Date Deposited: 06 Oct 2023 13:40
Last Modified: 06 Oct 2023 13:40
URI: http://journal.send2sub.com/id/eprint/2193

Actions (login required)

View Item
View Item