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Abstract

Neurodegenerative diseases such as Alzheimer’s, Parkinson’s, and Huntington’s are characterized by the accumulation of misfolded proteins in the brain, leading to neuronal dysfunction and eventual cell death. Understanding the intricate mechanisms governing protein folding and misfolding is crucial for developing effective therapeutic strategies. This review article delves into the fundamental processes of protein folding, the factors influencing protein misfolding, and the consequences of misfolded protein aggregation in neurodegenerative disorders. Various molecular mechanisms implicated in protein misfolding, including genetic mutations, environmental factors, and post-translational modifications, are discussed. Furthermore, we explore emerging research on the role of chaperone proteins, proteostasis networks, and cellular quality control mechanisms in maintaining protein homeostasis and preventing neurodegeneration. Insights gained from this exploration highlight promising avenues for future research and therapeutic interventions aimed at mitigating protein misfolding in neurodegenerative diseases.