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New Publication Identifies Key Proteins Involved in Amyloid Oligomer Binding and Supports Mechanism of CT1812
NEW YORK, Feb. 06, 2024 (GLOBE NEWSWIRE) -- Cognition Therapeutics, Inc. (NASDAQ: CGTX), a clinical stage company developing drugs that treat
About this update from Cognition Therapeutics, Inc.
[{"type":"text","content":"NEW YORK, Feb. 06, 2024 (GLOBE NEWSWIRE) -- Cognition Therapeutics, Inc. (NASDAQ: CGTX), a clinical stage company developing drugs that treat neurodegenerative disorders, announced that collaborators at the University of Edinburgh, Scotland published findings in the journal, Acta Neuropathologica, (doi: 10.1007/s00401-023-02679-6) that provide new insight into the biology of Alzheimer’s disease that is consistent with our understanding of the role the σ-2 receptor has in regulating Aβ oligomer binding. Using a combination of two high-resolution microscopy techniques: array tomography and Förster resonance energy transfer (FRET), Professor Tara Spires-Jones and colleagues at the UK Dementia Research Institute at University of Edinburgh’s Centre for Discovery Brain Sciences analyzed protein-protein interactions in over 1 million individual synapses in brain samples from people who had died with Alzheimer’s disease. Results detected TMEM97, a protein component of the σ-2 receptor complex, in close proximity to cellular prion protein (PrPc) on Alzheimer’s brain synapses. In addition, results found that Aβ oligomers were proximate to both PrPc, which has been shown to bind Aβ oligomers in neuronal cultures, as well as to TMEM97. These findings support the hypothesis that these receptor proteins may form a complex on the synapse surface with Aβ oligomers binding to one or both proteins. “Losing synaptic connections in the brain contributes to Alzheimer’s disease symptoms,” explained Professor Spires-Jones. “Previous work indicated that Aβ oligomers damage synapses, but until now it was not possible to know which proteins bind toxic forms of Aβ in human synapses. Combining FRET and array tomography imaging overcomes the limits of traditional microscopy and lets us determine whether proteins are close enough to interact in human brain samples. In simplest terms, while we had previous evidence that certain proteins existed in the same cellular neighborhood, we couldn’t precisely determine until now which houses were next to one another. Our findings help clarify the specific interactions between Aβ oligomers and synaptic receptors, which we hope will provide valuable information for drug developers.” Professor Spires-Jones' work also confirmed that in the presence of CT1812, Cognition’s lead product candidate, Aβ oligomers are displaced ...