Summary
Neurodegenerative diseases like Alzheimer's and Parkinson's are driven by the progressive buildup of toxic protein aggregates that disrupt neurons and cause widespread cell death. Current treatments fail to address this root cause, and existing biological disaggregation systems are heavily energy dependent, a serious limitation given that affected neurons already suffer from severe metabolic deficits.
CyP40 offers a differentiated approach by targeting and dissolving neurotoxic amyloid fibrils through proline isomerization, destabilizing their rigid structures and clearing neurofibrillary tangles. Unlike existing disaggregation systems, CyP40 operates entirely without ATP or cellular co-factors, making it energy efficient and better suited to the metabolic environment of diseased neurons. Its selective action targets only disease-relevant fibrils, avoiding disruption to normal protein folding. It can be delivered via polypeptide, polynucleotides, or viral vectors for localized brain expression.
Image shows CyP40 significantly lowered level of tau and promoted neuronal health in a mouse model overexpressing P301L tau
Desired Partnerships