Oxidative Stress, Mitochondrial Abnormalities and Proteins Deposition: Multitarget Approaches in Alzheimer's Disease

Title:Oxidative Stress, Mitochondrial Abnormalities and Proteins Deposition: Multitarget Approaches in Alzheimer's Disease

Volume: 17 Issue: 27

Author(s): Giulia Nesi, Simona Sestito, Maria Digiacomo and Simona Rapposelli*

Affiliation:

• Department of Pharmacy, University of Pisa, Via Bonanno 6, 56126 Pisa,Italy

Keywords: Alzheimer diseases, Oxidative stress, Multitarget-ligand, Neurodegeneration, AD therapy, Hybrid scaffold.

Abstract: Alzheimer Diseases (AD) is a multifactorial pathology characterized by a complex etiology. The hallmarks of AD, such as Aβ deposits in senile plaque and Neurofibrillary Tangles (NFT), are strongly intertwined with Reactive Oxygen Species (ROS) production and oxidative stress (OS), which are considered the common effectors of the cascade of degenerative events. An increasing body of evidence reveals that both mitochondrial abnormalities and metal accumulations synergistically act as major producers of ROS, thus contributing to neuronal toxicity. Consequently, the detrimental role of ROS production together with the neurodegenerative events involved in AD has been widely investigated as new potential therapeutic strategies. This review will concisely summarize the link between OS and the hallmarks of AD, emphasizing on their strong correlation with neurodegenerative events and elucidating the pivotal role of ROS in AD pathology. Furthermore, through this review, we will provide a short account of some of the efforts, challenges and opportunities in developing multitarget drugs by addressing ROS production, metal accumulation and protein depositions.

Cite this article as:

Nesi Giulia , Sestito Simona , Digiacomo Maria and Rapposelli Simona *, Oxidative Stress, Mitochondrial Abnormalities and Proteins Deposition: Multitarget Approaches in Alzheimer's Disease, Current Topics in Medicinal Chemistry 2017; 17 (27) . https://dx.doi.org/10.2174/1568026617666170607114232