Knowledge and Structure-Based Drug Design of 15-PGDH Inhibitors

  • J Med Chem. 2025 Sep 11;68(17):18436-18462. doi: 10.1021/acs.jmedchem.5c01231.
Leela S Dodda  1 Sebastien Campos  2 David Ciccone  1 Samantha Carreiro  1 Silvana Leit  1 Debra Brennan  1 Jacqueto Zephyr  1 Suzanne Jacques-O'Hagan  1 Sheetal Kumar  1 Fu-Shan Kuo  1 Md Munan Shaik  1 Daniel J Price  1 Christine Loh  1 Scott D Edmondson  1 Peter Tummino  1 Neelu Kaila  1
Affiliations
  • 1. Nimbus Therapeutics, Boston, Massachusetts 02210, United States.
  • 2. Pharmaron, Hoddesdon EN119FH, U.K.
Abstract

PGE2 plays important roles in immune cell function and in potentiating tissue regeneration. 15-PGDH is the key enzyme involved in inactivation of PGE2 and its inhibition therefore provides valuable therapeutic opportunity. We have solved the first cocrystal structure of 15-PGDH bound to small molecule inhibitors, enabling us to efficiently investigate and understand the key functionalities required for potency. Rational structure-based design coupled with a host of advanced computational methods, including FEP+ and WaterMap, were used to develop novel series of 15-PGDH inhibitors. Of note, a machine-learning (ML) model trained with potencies predicted by FEP+ yielded a powerful tool to guide synthetic priority across a large virtual chemical library. Ultimately, a lead compound demonstrated elevation of colonic PGE2 following IP administration in mice, consistent with our therapeutic hypothesis.

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