AbbVie Ends Partnership With BioArctic For Parkinson's Disease

AbbVie is ending an alpha-synuclein antibody collaboration agreement with BioArctic on Parkinson's disease and other movement disorders, according to the latest news.

At present, AbbVie has not released the relevant statement on its official website, but BioArctic has officially announced the news through a press release. In 2016, the two companies entered into a research collaboration agreement to co-develop and commercialize a combination of BioArcti's potential therapeutics for Parkinson's disease. Food is one of the hallmarks of Parkinson's disease.

In 2019, the two companies began a Phase I trial of ABBV-0805, with positive trial results announced at an international meeting in 2021. In addition, the U.S. FDA also approved its investigational new drug (IND) application shortly before the trial began. At present, the specific details of the termination of cooperation between the two parties have not been disclosed.

It is reported that ABBV-0805, also previously known as BAN0805, is not only studied for Parkinson's disease, but its indications also include other movement disorders, such as multiple system atrophy and dementia with Lewy bodies. The collaboration is primarily to find and develop a new therapy that can slow or stop the progression of Parkinson's disease.

The last data update for ABBV-0805 was in November 2021, when BioArctic shared preclinical data demonstrating the drug's ability to selectively target soluble, toxic α-synuclein aggregates.

In addition, AbbVie conducted a Phase I trial in March 2020 to test its safety and tolerability in 32 participants with idiopathic, mild-to-moderate Parkinson's disease, but was later terminated with The study was suspended for "strategic considerations".

While AbbVie is pulling out, Novartis has recently been confident in the development of alpha-synuclein drugs. Late last year, Novartis paid UCB up to $150 million in upfront payments and promised a potential $1.5 billion milestone to jointly develop a small-molecule inhibitor of alpha-synuclein misfolding.