Original discoveries in biophysics and biochemistry by our founders and scientists are the foundation for the company’s drug discovery platform targeting the fleeting protein intermediates in neurodegeneration.


  1. We demonstrated a highly reproducible and scalable in vitro assay platform for probing protein aggregation. We showed, for the first time, that it is possible to obtain highly reproducible measurements of aggregation kinetics for amyloid-beta (the “peptide from hell”).
    "Amyloid β-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process"
  2. We defined the previously intractable biophysical and mathematical rules of amyloid formation, including the dynamics of the toxic fleeting intermediates (oligomers). (a) We defined the rules of amyloid-beta aggregation for the first time, unmasking the molecular pathway that generates oligomers, and (b) we revealed, in molecular detail, the dynamics of oligomer populations formed during amyloid-beta aggregation.
    "Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism"
    "Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide"
  3. We discovered the rules that goven the function of nature’s own defenses (chaperones) and how they selectively interfere with amyloid formation and impede the formation of oligomers. We identified the first molecular chaperone to selectively interfere with amyloid-beta assembly and impede the formation of oligomers.
    "A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers"
  4. We developed tools to identify and optimize small molecules with a similar molecular mechanism to inhibit the generation of oligomers. We defined a framework for identifying and optimizing small molecule inhibitors of oligomer formation.
    "SAR by kinetics for drug discovery in protein misfolding diseases"
  5. We demonstrated that antibodies targeting plaque in Alzheimer's disease that haven’t been designed to block the formation of toxic oligomers specifically are “hit or miss” for inhibiting oligomers directly. We compared 4 clinical stage antibodies and show that only one of these directly inhibits the production of oligomers.
    "Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies"

Our team has >1,000 articles published in the world's leading scientific journals