On April 29, 2025 Blacksmith Medicines, Inc. (Blacksmith), a leading biopharma dedicated to discovering and developing therapeutics targeting metalloenzymes, reported the company will present 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 American Association for Cancer Research (AACR) (Free AACR Whitepaper) Annual Meeting 2025, taking place April 25-30 at the McCormick Place Convention Center, Chicago, IL (Press release, Blacksmith Medicines, APR 29, 2025, View Source [SID1234652304]).
Schedule your 30 min Free 1stOncology Demo!
Discover why more than 1,500 members use 1stOncology™ to excel in:
Early/Late Stage Pipeline Development - Target Scouting - Clinical Biomarkers - Indication Selection & Expansion - BD&L Contacts - Conference Reports - Combinatorial Drug Settings - Companion Diagnostics - Drug Repositioning - First-in-class Analysis - Competitive Analysis - Deals & Licensing
Schedule Your 30 min Free Demo!
Details of the poster presentation are as follows:
Abstract Number: 5720
Title: "Novel FEN1 nuclease inhibitor shows synergy with PARP-targeting drugs"
Session Category: Experimental and Molecular Therapeutics
Session Title: PARP Inhibitors
Session Date and Time: Tuesday April 29, 2025 2:00 PM – 5:00 PM
Location: Poster Section 24
Poster Board Number: 7
The abstract is now available on the conference website at AACR (Free AACR Whitepaper) Annual Meeting 2025.
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.