Future Direction of Designing Antioxidant Polymers in Modulating Protein Aggregation Process

Abstract

Amyloids are highly ordered aggregates of misfolded proteins, related to a large number of neurodegenerative diseases including Alzheimer’s, Parkinson’s, type II diabetes and many other debilitating disorders. The misfolded proteins are most commonly [Formula: see text]-sheet rich fibrillar aggregates, and one of the most common therapeutic approaches for the treatment of these disorders is inhibiting the formation of fibrillar aggregates. To date, a myriad of compounds have been introduced for this purpose, however poor water solubility and low bioavailability are major restrictions to achieve this purpose. To overcome these limitations, polymeric materials could be a great choice because of their many unique properties. Furthermore, oxidative stress is a key factor associated with the aforementioned disorders. In this context, natural polyphenolic compounds are attracting attention due to their abundance, potential antioxidant activities and nontoxic nature. Considering the importance of antioxidant agents in preventing the protein aggregation process, the design of novel antioxidant polymers has become a challenging task nowadays. Based on these perspectives, this review aims to provide an overall idea about the protein misfolding process, mechanistic pathway, and therapeutic approaches. The main focus of this review is the use of antioxidant molecules and the integration of natural polyphenol-based antioxidants with polymers for designing next-generation potential anti-amyloidogenic agents.