On January 27, 2025 Blacksmith Medicines, Inc. (Blacksmith), a leading biopharma dedicated to discovering and developing medicines targeting metalloenzymes, reported that it will present preclinical data on its oncology program targeting flap endonuclease 1 (FEN1), a structure-specific metallonuclease that cleaves 5’ DNA flaps during replication and repair, at the 8th DDR Inhibitors Summit taking place January 28th – 30th in Boston, MA (Press release, Blacksmith Medicines, JAN 27, 2025, View Source [SID1234649882]).
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"We are excited to have the opportunity to present an update on our novel FEN1 inhibitor program at the DDR Inhibitor Summit," said Zachary Zimmerman, Ph.D., CEO and co-founder of Blacksmith. "During the presentation we will highlight strong synergy between our novel FEN1 inhibitor and existing DDR drug classes underscoring its potential to enhance the therapeutic effects of existing DDR-targeting treatments."
Presentation details
Title: Novel FEN1 Inhibitor with Unique Metal-Binding Pharmacophore to Enhance Synergistic Therapeutic Effects with USP1, PARP, PARG, & ATR Inhibitors
Date/Time: January 30 @ 9:00am ET
Location: Hilton Boston Back Bay, Boston, MA
About FEN1
Flap endonuclease 1 (FEN1) is a structure-specific di-magnesium metallonuclease that cleaves 5’ DNA flaps during replication and repair. FEN1 is an attractive target for development of anticancer therapeutics because it is overexpressed in many tumor types and has a large number of synthetic lethality partners including genes in Homologous Recombination (HR) pathway.
About metalloenzymes and the Blacksmith platform
Metalloenzymes utilize a metal ion cofactor in the enzyme active site to perform essential biological functions. This diverse class of targets has historically been difficult to drug due to small molecule chemistry limitations that have plagued the industry. The Blacksmith metalloenzyme platform has solved this problem by leveraging the following:
A large proprietary fragment library of metal-binding pharmacophores (MBPs);
A comprehensive database containing a full characterization of the metalloenzyme genome including functions, metal cofactors, and associations to disease;
A first-of-its-kind metallo-CRISPR library of custom single guide RNAs;
An industry-leading metalloenzyme computational toolkit for docking, modeling and structure-based drug design; and
A robust and blocking intellectual property estate covering bioinorganic, medicinal, and computational chemistry approaches for metalloenzyme-targeted medicines.