Inhibit brain inflammation processes involved in disease pathogenesis

Misfolded protein aggregates can drive pathogenic processes underlying neurodegeneration via direct effects on neuronal cell function and by indirect actions through the chronic pathological activation of innate immune responses in astrocytes and microglia. Aggregated forms of amyloid beta, alpha-synuclein and huntingtin protein can activate the innate immune system to produce chronic inflammatory conditions that contribute to neurotoxicity. Recent studies have shown that chronic inflammatory states may not only meditate the toxicity of misfolded proteins, but also may serve as an early catalyst to the pathogenesis of neurodegenerative disease by impairing protein clearance mechanisms and increasing protein aggregation. Thus, targeting disease-associated neuroinflammation may confer multiple benefits, including mitigation of the toxicity of misfolded proteins in an established disease state, and restoration of protein clearance mechanisms to slow the disease progression. Neuropore Therapies has two programs (NPT520-34 and TLR2 antagonist) which target the neuroinflammatory components of neurodegenerative disorders.