| Literature DB >> 28471663 |
Martin W Rowbottom1, Gretchen Bain1, Imelda Calderon1, Taylor Lasof1, David Lonergan1, Andiliy Lai1, Fei Huang1, Janice Darlington1, Patricia Prodanovich1, Angelina M Santini1, Christopher D King1, Lance Goulet1, Kristen E Shannon1, Gina L Ma1, Katherine Nguyen1, Deidre A MacKenna1, Jilly F Evans1, John H Hutchinson1.
Abstract
LOXL2 catalyzes the oxidative deamination of ε-amines of lysine and hydroxylysine residues within collagen and elastin, generating reactive aldehydes (allysine). Condensation with other allysines or lysines drives the formation of inter- and intramolecular cross-linkages, a process critical for the remodeling of the ECM. Dysregulation of this process can lead to fibrosis, and LOXL2 is known to be upregulated in fibrotic tissue. Small-molecules that directly inhibit LOXL2 catalytic activity represent a useful option for the treatment of fibrosis. Herein, we describe optimization of an initial hit 2, resulting in identification of racemic-trans-(3-((4-(aminomethyl)-6-(trifluoromethyl)pyridin-2-yl)oxy)phenyl)(3-fluoro-4-hydroxypyrrolidin-1-yl)methanone 28, a potent irreversible inhibitor of LOXL2 that is highly selective over LOX and other amine oxidases. Oral administration of 28 significantly reduced fibrosis in a 14-day mouse lung bleomycin model. The (R,R)-enantiomer 43 (PAT-1251) was selected as the clinical compound which has progressed into healthy volunteer Phase 1 trials, making it the "first-in-class" small-molecule LOXL2 inhibitor to enter clinical development.Entities:
Mesh:
Substances:
Year: 2017 PMID: 28471663 DOI: 10.1021/acs.jmedchem.7b00345
Source DB: PubMed Journal: J Med Chem ISSN: 0022-2623 Impact factor: 7.446