Targeted Protein Structures of Hell (Patreon)

Amyloid protofibrils, amyloid fibrils, and amyloid oligomers are all types of protein structures that are associated with neurodegenerative diseases such as Alzheimer's and Parkinson's diseases.

Amyloid protofibrils are intermediate structures that form during the aggregation of amyloid proteins. They are smaller and more soluble than mature amyloid fibrils and are thought to be more toxic to cells.

Amyloid fibrils are long, insoluble fibers that result from the aggregation of amyloid proteins. These fibrils are a hallmark of amyloid diseases and are thought to contribute to the progression of these diseases by forming toxic plaques in the brain.

Amyloid oligomers are small, soluble aggregates of amyloid proteins that are thought to be particularly toxic to cells. They can disrupt cell membranes, interfere with neurotransmission, and induce cell death.

Prion scrapies, on the other hand, are infectious proteins that can cause a group of diseases known as transmissible spongiform encephalopathies (TSEs). These diseases include scrapie in sheep, mad cow disease in cattle, and Creutzfeldt-Jakob disease in humans. Prion scrapies are thought to misfold normal proteins in the brain, leading to the formation of aggregates and ultimately causing neurodegeneration.