Protein aggregation pathology

Protein aggregation pathology is characterized by the accumulation and clumping of misfolded or intrinsically disordered proteins within or outside cells. This phenomenon plays a fundamental role in disease mechanisms, particularly in neurodegenerative conditions such as amyotrophic lateral sclerosis (ALS), Alzheimer’s disease, Parkinson’s disease, and prion diseases[6][4][5][3]. Aggregation most often results from disturbances in protein folding and proteostasis networks, leading to the formation of toxic protein species that can injure or kill cells[5][6]. The study and therapeutic targeting of protein aggregation pathways (for example, using gene silencing, small molecules, chaperones, and antibodies) represents a major strategy in modern medicine, both in disease modification and in improving the safety and efficacy of biopharmaceutical products[2][6][1]. Safety concerns include immunogenic responses to aggregates and the difficulty in selectively targeting pathological, rather than physiological, aggregation[1][5].

Other names

Protein aggregationProtein misfolding pathologyPathological protein deposition

Suppression or modulation of aggregation-prone proteins (gene silencing, antisense therapy) Enhancement of cellular clearance mechanisms (proteasomes, autophagy) Stabilization or refolding of misfolded proteins (chemical/chaperone modulation) Immunotherapies targeting aggregates (antibody neutralization)