amyloidbildning

Amyloidbildning, or amyloid formation, refers to the pathological accumulation of misfolded protein aggregates in tissues or organs. These aggregates, known as amyloids, have a characteristic cross‑beta sheet structure that can be visualized by staining with Congo red or thioflavin T, which bind specifically to the fibrillar architecture. Amyloid deposits are associated with a spectrum of diseases, from neurodegenerative disorders such as Alzheimer’s disease, where β‑amyloid peptides accumulate in the brain, to systemic conditions like primary amyloidosis (AL) in which immunoglobulin light chains form deposits in multiple organs. The process is driven by protein misfolding, nucleation, and fibril growth, often exacerbated by genetic mutations, environmental factors, or impaired cellular clearance mechanisms.

In neurodegenerative contexts, amyloid plaques are typically surrounded by neuroinflammatory responses and synaptic dysfunction, contributing to cognitive decline. In systemic amyloidosis, the deposition pattern depends on the precursor protein; for example, transthyretin (ATTR) amyloidosis affects heart and peripheral nerves, whereas serum amyloid A (AA) amyloidosis is linked to chronic inflammatory states. Diagnosis relies on imaging, biopsy of accessible tissue, and biomarker analysis, with emerging techniques like positron emission tomography ligands improving detection.

Therapeutic strategies target various stages of amyloidogenesis. Small molecules, antibodies, and protein chaperones aim to inhibit aggregation, promote disaggregation, or enhance clearance by the immune system. Gene‑editing approaches such as antisense oligonucleotides reduce the production of amyloidogenic proteins, showing promise in conditions like ATTR cardiomyopathy. Early recognition and intervention remain critical, as amyloid deposition is often progressive and irreversible, underscoring the importance of ongoing research into prevention, diagnosis, and treatment.