The amyloid-forming proteins tau, αB crystallin, and amyloid P protein are all 
found in lesions of multiple sclerosis (MS). Our previous work established that 
amyloidogenic peptides from the small heat shock protein αB crystallin (HspB5) 
and from amyloid β fibrils, characteristic of Alzheimer's disease, were 
therapeutic in experimental autoimmune encephalomyelitis (EAE), reflecting 
aspects of the pathology of MS. To understand the molecular basis for the 
therapeutic effect, we showed a set of amyloidogenic peptides composed of six 
amino acids, including those from tau, amyloid β A4, major prion protein (PrP), 
HspB5, amylin, serum amyloid P, and insulin B chain, to be anti-inflammatory and 
capable of reducing serological levels of interleukin-6 and attenuating 
paralysis in EAE. The chaperone function of the fibrils correlates with the 
therapeutic outcome. Fibrils composed of tau 623-628 precipitated 49 plasma 
proteins, including apolipoprotein B-100, clusterin, transthyretin, and 
complement C3, supporting the hypothesis that the fibrils are active biological 
agents. Amyloid fibrils thus may provide benefit in MS and other 
neuroinflammatory disorders.