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Apr 01, 2010
 |  BC Innovations  |  Targets & Mechanisms

Affibody vs Amyloid

Swedish and British researchers have shown that Affibody AB's Affibodies can be engineered to bind and clear toxic b-amyloid from the brains of fruit flies.1 The academics are now planning to look at the Affibodies in rodent models of Alzheimer's disease.

The biotech is helping by increasing the bioavailability of its lead Affibody for AD, ZAb3, but its focus remains on Affibodies for cancer.

High levels of b-amyloid (Ab) peptide in the brain, from either overproduction of the peptide or failure to clear it, are thought to lead to widespread Ab aggregates and plaques. These in turn cause neuronal and synaptic dysfunction and, ultimately, learning and memory deficits.

Because excessive Ab sits at the top of the amyloid cascade, one strategy has been to target the peptide and prevent it from forming the oligomers and aggregates that trigger CNS dysfunction. There are at least 10 antibody and small molecule inhibitors of Ab aggregates in the clinic to treat AD.

Affibodies represent a third option, offering a lower risk of immunogenicity than antibodies and better binding affinity than small molecules. Although they are less than half the size of an antibody, Affibodies still share the latter᾽s strong binding affinity and stability.

Previously, structural biology professor Torleif Härd at the Swedish University of Agricultural Sciences, colleagues at the KTH Royal Institute of Technology and researchers at Affibody AB had identified an Affibody dimer that bound monomeric Ab with nanomolar affinity in vitro.2 Denoted ZAb3, the dimer...

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