Purpose of the Review <p>Protein aggregation involving misfolded proteins like alpha-synuclein (α-Syn), tau, and amyloid-beta is a key factor in neurodegenerative diseases such as Parkinson’s, Alzheimer’s, and Huntington’s. These aggregates disrupt cellular homeostasis and lead to neurotoxicity. Understanding their formation is crucial for developing disease modifying treatment.</p> Recent Findings <p>A literature review was performed using PubMed, Scopus, and Web of Science to identify studies on protein misfolding, aggregation, and related therapeutic strategies. Keywords related to protein aggregation, neurodegeneration, and interventions were used. Studies were selected based on innovation, relevance, and translational potential. Protein aggregation is influenced by genetic mutations, oxidative stress, proteostasis imbalance, and environmental factors. Promising therapies include molecular chaperones, aggregation inhibitors, autophagy enhancers, and immunotherapies. However, therapeutic translation is limited by issues such as blood-brain barrier permeability, off-target effects, and patient variability. New delivery systems and multi-targeted approaches are under investigation to improve outcomes.</p> Summary <p>Targeting protein aggregation is a promising but challenging approach for treating neurodegenerative diseases. Continued research into molecular mechanisms and therapeutic innovation is essential. Collaborative efforts integrating biology, pharmacology, and technology may lead to effective, clinically translatable therapies.</p>