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Design and synthesis of aminothiazole based Hepatitis B Virus (HBV) capsid inhibitors
- Source :
- European Journal of Medicinal Chemistry. 166:480-501
- Publication Year :
- 2019
- Publisher :
- Elsevier BV, 2019.
-
Abstract
- The capsid assembly is an essential step for Hepatitis B Virus (HBV) life cycle and is an important target for anti-HBV drug development. In this report, we identified a hit compound with aminothiazole structure by the high throughput screening (HTS) which inhibited the interaction of HBV capsid protein within the cells. The structure hopping and SAR studies of the hit compound afforded compound 79 with potent anti-HBV replication activity and good basic drug-like properties. The working mechanism studies showed that compound 79 could bind to the similar binding site of known HBV capsid inhibitor with heteroaryldihydropyrimidine (HAP) scaffold, through similar hydrophobic interactions but with a different hydrogen bond. This compound exerted potent inhibitory effect upon HBV production, either in cell culture or in mice with no obvious acute toxicity. We propose that further development of this compound could lead to novel potent anti-HBV inhibitors that target HBV capsid assembly.
- Subjects :
- Male
Hepatitis B virus
Protein Conformation
High-throughput screening
Drug Evaluation, Preclinical
Chemistry Techniques, Synthetic
Virus Replication
medicine.disease_cause
Antiviral Agents
01 natural sciences
Inhibitory Concentration 50
Mice
Structure-Activity Relationship
03 medical and health sciences
chemistry.chemical_compound
Protein structure
Aminothiazole
Drug Discovery
medicine
Animals
Humans
Structure–activity relationship
Binding site
030304 developmental biology
Pharmacology
0303 health sciences
010405 organic chemistry
Chemistry
Virus Assembly
Organic Chemistry
HEK 293 cells
virus diseases
Hep G2 Cells
General Medicine
Virology
digestive system diseases
High-Throughput Screening Assays
0104 chemical sciences
Molecular Docking Simulation
HEK293 Cells
Capsid
Capsid Proteins
Hydrophobic and Hydrophilic Interactions
Subjects
Details
- ISSN :
- 02235234
- Volume :
- 166
- Database :
- OpenAIRE
- Journal :
- European Journal of Medicinal Chemistry
- Accession number :
- edsair.doi.dedup.....26975932a6b9ada9c7580da394805448