| Literature DB >> 30034610 |
Lara S Kallander1, David Washburn1, Mark A Hilfiker1, Hilary Schenck Eidam1, Brian G Lawhorn1, Joanne Prendergast1, Ryan Fox1, Sarah Dowdell1, Sharada Manns1, Tram Hoang1, Steve Zhao1, Guosen Ye1, Marlys Hammond1, Dennis A Holt1, Theresa Roethke1, Xuan Hong1, Robert A Reid1, Robert Gampe1, Hong Zhang1, Elsie Diaz1, Alan R Rendina1, Amy M Quinn1, Bob Willette1.
Abstract
Bone Morphogenetic Protein 1 (BMP1) inhibition is a potential method for treating fibrosis because BMP1, a member of the zinc metalloprotease family, is required to convert pro-collagen to collagen. A novel class of reverse hydroxamate BMP1 inhibitors was discovered, and cocrystal structures with BMP1 were obtained. The observed binding mode is unique in that the small molecule occupies the nonprime side of the metalloprotease pocket providing an opportunity to build in metalloprotease selectivity. Structure-guided modification of the initial hit led to the identification of an oral in vivo tool compound with selectivity over other metalloproteases. Due to irreversible inhibition of cytochrome P450 3A4 for this chemical class, the risk of potential drug-drug interactions was managed by optimizing the series for subcutaneous injection.Entities:
Year: 2018 PMID: 30034610 PMCID: PMC6047045 DOI: 10.1021/acsmedchemlett.8b00173
Source DB: PubMed Journal: ACS Med Chem Lett ISSN: 1948-5875 Impact factor: 4.345