US-based Blacksmith Medicines has signed a merger agreement with Forge Therapeutics to develop and discover drugs that target a large class of proteins called metalloenzymes.
Based in California, Forge Therapeutics is involved in developing novel antibiotics that target bacterial metalloenzymes.
As per the deal, both firms will use their combined chemistry platforms to create a biopharma that will develop these drugs. Initially, the enlarged company will focus on oncology and infection.
Blacksmith Medicines CEO and co-founder Zachary Zimmerman said: “We are excited to unveil the merger of Blacksmith and Forge, which we believe will be transformational for both companies.
“Prospects are very bright for the new Blacksmith, as we are now able to expand our metalloenzyme platform, advance our internal and partnered programs, and create increased value for our shareholders by discovering first-in-class and best-in-class medicines.
“Our target strategy is to focus on metalloenzymes of significant unmet need and high pharma interest, targets with validated biology that have been challenging to drug due to chemistry limitations that we can solve with our platform.”
According to Blacksmith Medicines, its metalloenzyme platform has a large proprietary fragment library of metal-binding pharmacophores (MBPs) and a database of full characterisation of the metalloenzyme genome.
The platform uses a metalloenzyme computational toolkit for docking, modelling, and structure-based drug design and a metallo-CRISPR library of custom single-guide RNAs.
It is supported by pharmaceutical collaborations with Switzerland-based Roche, Eli Lilly, and Basilea. These deals have the potential to generate over $800m in milestone payments plus royalties, the US-based pharma firm added.
Additionally, the business has received non-dilutive federal funding of up to $25.3m, which will enable it to completely fund its programmes in infectious diseases through phase 1.
Furthermore, Blacksmith Medicines is developing programmes for precision oncology that target new synthetic lethality targets connected to the DNA damage response.