Tau-aggregation inhibition: promising role of nanoencapsulated dietary molecules in the management of Alzheimer’s disease.

Pramod, G. Nagaraju and Ashwini, S. and Poornima Priyadarshini, C. G. (2022) Tau-aggregation inhibition: promising role of nanoencapsulated dietary molecules in the management of Alzheimer’s disease. Critical Reviews in Food Science and Nutrition. ISSN 1549-7852

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Abstract

Alzheimer’s disease (AD) is a cumulative form of dementia associated with memory loss, cognition impairment, and finally leading to death. AD is characterized by abnormal deposits of extracellular beta-amyloid and intracellular Tau-protein tangles throughout the brain. During pathological conditions of AD, Tau protein undergoes various modifications and aggregates over time. A number of clinical trials on patients with AD symptoms have indicated the effectiveness of Tau-based therapies over anti-Aβ treatments. Thus, there is a huge paradigm shift toward Tau aggregation inhibitors. Several bioactives of plants and microbes have been suggested to cross the neuronal cell membrane and play a crucial role in managing neurodegenerative disorders. Bioactives mainly act as active modulators of AD pathology besides having antioxidant and anti-inflammatory potential. Studies also demonstrated the potential role of dietary molecules in inhibiting the formation of Tau aggregates and removing toxic Tau. Further, these molecules in nonencapsulated form exert enhanced Tau aggregation inhibition activity both in in vitro and in vivo studies suggesting a remarkable role of nanoencapsulation in AD management. The present article aims to review and discuss the structure-function relationship of Tau protein, the post-translational modifications that aid Tau aggregation and potential bioactives that inhibit Tau aggregation.

Item Type:	Article
Uncontrolled Keywords:	Alzheimer’s disease; blood-brain barrier; dietary molecules; nanomolecules; nanotechnology; tau protein aggregates
Subjects:	500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 29 Protein Chemistry 600 Technology > 01 Medical sciences > 09 Human Physiology
Divisions:	Molecular Nutrition
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	22 May 2023 08:47
Last Modified:	22 May 2023 08:47
URI:	http://ir.cftri.res.in/id/eprint/16435

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