The First Potent Inhibitor of Mammalian Group X Secreted Phospholipase A2: Elucidation of Sites for Enhanced Binding
BP Smart, RC Oslund, LA Walsh… - Journal of medicinal …, 2006 - ACS Publications
Using the X-ray structure of human group X secreted phospholipase A2 (hGX), we carried
out structure-based design of indole-based inhibitors and prepared the compounds using a
new synthetic route. The most potent compound inhibited hGX and the mouse orthologue
with an IC50 of 75 nM. This compound is the most potent hGX inhibitor reported to date and
was also found to inhibit a subset of the other mouse and human sPLA2s.
out structure-based design of indole-based inhibitors and prepared the compounds using a
new synthetic route. The most potent compound inhibited hGX and the mouse orthologue
with an IC50 of 75 nM. This compound is the most potent hGX inhibitor reported to date and
was also found to inhibit a subset of the other mouse and human sPLA2s.
Using the X-ray structure of human group X secreted phospholipase A2 (hGX), we carried out structure-based design of indole-based inhibitors and prepared the compounds using a new synthetic route. The most potent compound inhibited hGX and the mouse orthologue with an IC50 of 75 nM. This compound is the most potent hGX inhibitor reported to date and was also found to inhibit a subset of the other mouse and human sPLA2s.
ACS Publications