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Amyloid Fibril Formation (N/A)
- Target
- N/A
- Molecular classification
- Protein aggregation, Self-assembling protein structures
01
Overview
Amyloid fibril formation is the process by which normally soluble proteins misfold and aggregate into highly ordered, insoluble fibrillar structures known as amyloid fibrils. These fibrils are characterized by their resistance to proteolysis, insolubility in aqueous solutions, and a distinctive cross-β X-ray diffraction pattern. Amyloid formation is implicated in numerous diseases (amyloidoses), including Alzheimer's disease, Parkinson's disease, type 2 diabetes (islet amyloidosis), and systemic amyloidoses such as light chain (AL) or transthyretin (ATTR) amyloidosis. Targeting amyloid fibril formation is a therapeutic strategy for these diseases.
- Other names
- AmyloidogenesisAmyloid aggregationFibrillogenesis
02
Mechanism of action
Inhibition of amyloid aggregation, promotion of amyloid clearance, stabilization of native protein conformation
03
Biological functions
Protein misfoldingProtein aggregationCell deathTissue disruption
04
Disease associations
Alzheimer's diseaseParkinson's diseaseType 2 diabetesAmyloidosisNeurodegenerative diseaseSystemic amyloidosis
05
Safety considerations
Off-target effects of anti-amyloid agentsAdverse immune responses to amyloid antibodiesARIA (Amyloid-Related Imaging Abnormalities) in clinical trials
06
Interacting drugs
Thioflavin T
2 more in the full profile.
07
Biomarkers
Amyloid plaques (imaging)Amyloid levels in cerebrospinal fluid (CSF)Plasma amyloid levels
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