2. Academic Validation
  3. The development of highly potent inhibitors for porcupine

The development of highly potent inhibitors for porcupine

  • J Med Chem. 2013 Mar 28;56(6):2700-4. doi: 10.1021/jm400159c.
Xiaolei Wang 1,  Jesung Moon,  Michael E Dodge,  Xinchao Pan,  Lishu Zhang,  Jordan M Hanson,  Rubina Tuladhar,  Zhiqiang Ma,  Heping Shi,  Noelle S Williams,  James F Amatruda,  Thomas J Carroll,  Lawrence Lum,  Chuo Chen
Affiliations

Affiliation

  • 1 Department of Biochemistry, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390, USA.
PMID: 23477365 DOI: 10.1021/jm400159c
Abstract

Porcupine is a member of the membrane-bound O-acyltransferase family of proteins. It catalyzes the palmitoylation of Wnt proteins, a process required for their secretion and activity. We recently disclosed a class of small molecules (IWPs) as the first reported Porcn inhibitors. We now describe the structure-activity relationship studies and the identification of subnanomolar inhibitors. We also report herein the effects of IWPs on Wnt-dependent developmental processes, including zebrafish posterior axis formation and kidney tubule formation.

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