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Amyloid Fibril (N/A)
- Target
- N/A
- Molecular classification
- Protein aggregate, Supramolecular assembly
01
Overview
Amyloid fibrils are insoluble, highly ordered protein aggregates characterized by a distinctive fibrillar morphology and a cross-β-sheet secondary structure. They form when normally soluble proteins misfold and assemble into long, unbranched fibers that are resistant to degradation. These structures are implicated in various diseases (such as Alzheimer's disease, type 2 diabetes, and prion diseases) but can also have functional roles in some biological contexts.
- Other names
- Amyloid aggregateAmyloid depositCross-beta structureAmyloid plaque
02
Mechanism of action
N/A
03
Biological functions
Protein aggregationSelf-assemblyStructural component (in some cases)Biofilm formation (in some cases)
04
Disease associations
Neurodegenerative diseaseAlzheimer's diseaseParkinson's diseaseType 2 diabetesPrion diseasesSystemic amyloidosis
05
Safety considerations
ImmunogenicityOff-target effectsIncomplete removal of amyloidAcceleration of disease progression (in some cases)Inflammation
06
Biomarkers
Amyloid-beta (Aβ) levels in cerebrospinal fluid (CSF)Amyloid PET imaging
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