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Discovery of a Hepatitis C Virus NS5B Replicase Palm Site Allosteric Inhibitor (BMS-929075) Advanced to Phase 1 Clinical Studies
- Source :
- Journal of Medicinal Chemistry. 60:4369-4385
- Publication Year :
- 2017
- Publisher :
- American Chemical Society (ACS), 2017.
-
Abstract
- The hepatitis C virus (HCV) NS5B replicase is a prime target for the development of direct-acting antiviral drugs for the treatment of chronic HCV infection. Inspired by the overlay of bound structures of three structurally distinct NS5B palm site allosteric inhibitors, the high-throughput screening hit anthranilic acid 4, the known benzofuran analogue 5, and the benzothiadiazine derivative 6, an optimization process utilizing the simple benzofuran template 7 as a starting point for a fragment growing approach was pursued. A delicate balance of molecular properties achieved via disciplined lipophilicity changes was essential to achieve both high affinity binding and a stringent targeted absorption, distribution, metabolism, and excretion profile. These efforts led to the discovery of BMS-929075 (37), which maintained ligand efficiency relative to early leads, demonstrated efficacy in a triple combination regimen in HCV replicon cells, and exhibited consistently high oral bioavailability and pharmacokinetic parameters across preclinical animal species. The human PK properties from the Phase I clinical studies of 37 were better than anticipated and suggest promising potential for QD administration.
- Subjects :
- Male
0301 basic medicine
Hepatitis C virus
Allosteric regulation
RNA-dependent RNA polymerase
Hepacivirus
Viral Nonstructural Proteins
medicine.disease_cause
Antiviral Agents
01 natural sciences
Rats, Sprague-Dawley
03 medical and health sciences
chemistry.chemical_compound
Dogs
Allosteric Regulation
Drug Discovery
medicine
Animals
Humans
Benzofuran
NS5B
Benzofurans
Ligand efficiency
010405 organic chemistry
Chemistry
Drug discovery
Haplorhini
Hepatitis C
Rats
0104 chemical sciences
Molecular Docking Simulation
030104 developmental biology
Biochemistry
Benzothiadiazine
Molecular Medicine
Allosteric Site
Subjects
Details
- ISSN :
- 15204804 and 00222623
- Volume :
- 60
- Database :
- OpenAIRE
- Journal :
- Journal of Medicinal Chemistry
- Accession number :
- edsair.doi.dedup.....43e500f8c2cd73d6873f1280c193d753
- Full Text :
- https://doi.org/10.1021/acs.jmedchem.7b00328