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Drug Development.

Erika N Cline1, Elizabeth Johnson1, Martin Kleinschmidt2

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Alzheimer'S & Dementia : the Journal of the Alzheimer'S Association
|December 26, 2025
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Summary
This summary is machine-generated.

Sabirnetug demonstrates superior selectivity for toxic amyloid-beta oligomers (AβOs) over monomers in Alzheimer's disease (AD) research. This enhanced selectivity is crucial for effectively targeting AβOs in early AD and mild cognitive impairment (MCI).

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Area of Science:

  • Neuroscience
  • Immunology
  • Pharmacology

Background:

  • Sabirnetug (ACU193) is a monoclonal antibody targeting toxic soluble amyloid-beta oligomers (AβOs).
  • Its efficacy is under investigation for mild cognitive impairment (MCI) and early Alzheimer's disease (AD).
  • High selectivity for AβOs over monomers is key due to monomer abundance in MCI/AD.

Purpose of the Study:

  • To compare the binding affinities and selectivity of sabirnetug against other Aβ-targeting antibodies.
  • Evaluate sabirnetug's potential therapeutic advantage in targeting AβOs in AD.

Main Methods:

  • Recombinant production of lecanemab, aducanumab, and donanemab.
  • Surface plasmon resonance (SPR) used to determine binding kinetics to Aβ oligomers and monomers.
  • Comparison of binding affinities (KD) and selectivity ratios.

Main Results:

  • Sabirnetug exhibited the highest binding affinities to Aβ oligomers (ADDLs, Aβ1-42 oligomers).
  • Sabirnetug demonstrated significantly lower affinity for monomeric Aβ1-40, resulting in high selectivity.
  • Aducanumab and donanemab showed lower selectivity for AβOs over monomers.

Conclusions:

  • Sabirnetug displays superior selectivity for AβOs over monomeric Aβ compared to tested antibodies.
  • High selectivity positions sabirnetug favorably for targeting AβOs in MCI/AD.
  • Further investigation in ALTITUDE-AD (NCT06335173) is ongoing.