Unlock stock picks and a broker-level newsfeed that powers Wall Street.

ProMIS Neurosciences to Showcase PMN310’s Ability to Target Toxic Oligomers and Distinguish from Other Amyloid-Beta Oligomers in Preclinical Studies at the 4th International Conference on Cognitive & Behavioral Neurosciences

In This Article:

ProMIS Neurosciences Inc.
ProMIS Neurosciences Inc.

CAMBRIDGE, Massachusetts and TORONTO, Ontario, Sept. 12, 2024 (GLOBE NEWSWIRE) -- ProMIS Neurosciences Inc. (Nasdaq: PMN), a biotechnology company focused on the generation and development of antibody therapeutics targeting toxic misfolded proteins in neurodegenerative diseases such as Alzheimer’s disease (AD), amyotrophic lateral sclerosis (ALS) and multiple system atrophy (MSA), today announced that preclinical data supporting the potential role of its lead product candidate, PMN310, as a treatment for AD will be highlighted in an oral presentation at the 4th International Conference on Cognitive & Behavioral Neurosciences (ICBN) taking place from September 12-13, 2024 in Lisbon, Portugal.

A large body of evidence indicates that the most pathogenic species of amyloid-beta (Aß) in AD consists of soluble toxic oligomers as opposed to insoluble fibrils and monomers. The ability of a therapeutic antibody to target toxic amyloid-beta oligomers (AßO) without being diverted by binding to competing non-toxic species has the potential to result in greater efficacy. As a next generation antibody, PMN310 is a therapeutic candidate designed to target toxic oligomers more selectively.

“The data being shared at ICBN further support PMN310 as a potential treatment for AD due to its enhanced selectivity for toxic oligomers” stated Johanne Kaplan, Ph.D., Chief Development Officer of ProMIS Neurosciences and platform presenter. “Importantly, the ability of PMN310 to avoid interaction with plaque and vascular deposits of amyloid-beta could potentially reduce the risk of amyloid-related imaging abnormalities, or ARIA, a dose-limiting toxicity associated with plaque-binding antibodies.”

In the studies, the binding of PMN310 and other Aß-directed antibodies to a toxic oligomer-enriched low molecular fraction of brain extract from AD patients was evaluated by surface plasmon resonance, with and without monomer competition. The results indicated that PMN310 showed little or no interaction with monomers and was among the least impacted by excess monomer competition in binding to toxic oligomers in AD brain extract. Additionally, PMN310 did not bind to Aß plaque or vascular deposits as determined by immunohistochemistry. These results highlight how PMN310 distinguishes itself from other Aß-directed antibodies and may potentially provide an improved product profile with enhanced efficacy.

Details of the oral presentation are as follows:

Title: Distinguishing between amyloid-beta directed antibodies: Ability of PMN310 to target toxic oligomers despite competing species
Date/Time of Virtual Presentation: Friday, September 13 at 2:00pm WEST (6:00am PT / 9:00am ET)
Authors: Johanne Kaplan, Ebrima Gibbs, Juliane Coutts, Beibei Zhao, Neil R. Cashman