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@ARTICLE{Orsi:491342,
author = {Orsi, Douglas L. and Ferrara, Steven J. and Siegel, Stephan
and Friberg, Anders and Bouché, Léa and Pook, Elisabeth
and Lienau, Philip and Bluck, Joseph P. and Lemke,
Christopher T. and Akcay, Gizem and Stellfeld, Timo and
Meyer, Hanna and Pütter, Vera and Holton, Simon J. and
Korr, Daniel and Jerchel-Furau, Isabel and Pantelidou,
Constantia and Strathdee, Craig A. and Meyerson, Matthew and
Eis, Knut and Goldstein, Jonathan T.},
title = {{D}iscovery and characterization of orally bioavailable
4-chloro-6-fluoroisophthalamides as covalent {PPARG}
inverse-agonists},
journal = {Bioorganic $\&$ medicinal chemistry},
volume = {78},
issn = {0968-0896},
address = {Amsterdam [u.a.]},
publisher = {Elsevier},
reportid = {PUBDB-2023-00097},
pages = {117130},
year = {2023},
abstract = {PPAR gamma (PPARG) is a ligand activated transcription
factor that regulates genes involved in inflammation, bone
biology, lipid homeostasis, as well as a master regulator of
adipogenesis and a potential lineage driver of luminal
bladder cancer. While PPARG agonists lead to transcriptional
activation of canonical target genes, inverse agonists have
the opposite effect through inducing a transcriptionally
repressive complex leading to repression of canonical target
gene expression. While many agonists have been described and
tested clinically, inverse agonists offer an underexplored
avenue to modulate PPARG biology in vivo. Current inverse
agonists lack favorable in vivo properties; herein we
describe the discovery and characterization of a series of
orally bioavailable 4-chloro-6-fluoroisophthalamides as
covalent PPARG inverse-agonists, BAY-5516, BAY-5094, and
BAY-9683. Structural studies of this series revealed
distinct pre- and post-covalent binding positions, which led
to the hypothesis that interactions in the pre-covalent
conformation are primarily responsible for driving affinity,
while interactions in the post-covalent conformation are
more responsible for cellular functional effects by
enhancing PPARG interactions with its corepressors. The need
to simultaneously optimize for two distinct states may
partially explain the steep SAR observed. Exquisite
selectivity was achieved over related nuclear receptors in
the subfamily due in part to a covalent warhead with low
reactivity through an SNAr mechanism in addition to the
specificity gained through covalent binding to a reactive
cysteine uniquely positioned within the PPARG LBD. BAY-5516,
BAY-5094, and BAY-9683 lead to pharmacodynamic regulation of
PPARG target gene expression in vivo comparable to known
inverse agonist SR10221 and represent new tools for future
in vivo studies to explore their potential utility for
treatment of disorders of hyperactivated PPARG including
luminal bladder cancer and other disorders.},
cin = {EMBL-User},
ddc = {610},
cid = {I:(DE-H253)EMBL-User-20120814},
pnm = {6G3 - PETRA III (DESY) (POF4-6G3)},
pid = {G:(DE-HGF)POF4-6G3},
experiment = {EXP:(DE-H253)P-P14-20150101 / EXP:(DE-H253)P-P11-20150101},
typ = {PUB:(DE-HGF)16},
pubmed = {36542958},
UT = {WOS:000911046100001},
doi = {10.1016/j.bmc.2022.117130},
url = {https://bib-pubdb1.desy.de/record/491342},
}