Paritaprevir is an orally bioavailable, synthetic acylsulfonamide inhibitor of the hepatitis C virus (HCV) protease complex comprised of non-structural protein 3 and 4A (NS3/NS4A), with potential activity against HCV genotype 1.
CAT No: R2246
CAS No:1216941-48-8
Chemical Name:(1S,4R,6S,7Z,14S,18R)-N-cyclopropylsulfonyl-14-[(5-methylpyrazine-2-carbonyl)amino]-2,15-dioxo-18-phenanthridin-6-yloxy-3,16-diazatricyclo[14.3.0.04,6]nonadec-7-ene-4-carboxamide
Paritaprevir is a synthetic small-molecule inhibitor belonging to the class of direct-acting antiviral (DAA) agents, specifically designed to target viral proteases. As an acylsulfonamide-containing compound, it is structurally tailored to inhibit the NS3/4A serine protease of hepatitis C virus (HCV), a critical enzyme responsible for viral polyprotein processing and replication. Its high affinity for the viral protease and selectivity over host proteases have made it a valuable tool compound in virology and antiviral drug discovery. The unique chemical features and potent inhibitory activity of Paritaprevir have positioned it as an important molecule for research focused on understanding viral replication mechanisms, resistance development, and the broader landscape of protease inhibitor pharmacology.
Antiviral Mechanism Studies: Paritaprevir serves as a model compound for elucidating the mechanistic details of HCV NS3/4A protease inhibition. Researchers utilize it to probe the structural and kinetic aspects of enzyme inhibition, enabling a deeper understanding of how acylsulfonamide-based inhibitors engage with the protease active site. Such studies are fundamental for mapping the conformational dynamics of the viral protease and for identifying key residues involved in inhibitor binding, which in turn inform the rational design of next-generation antiviral agents.
Drug Resistance Research: The compound is widely employed in laboratory models to investigate the emergence and molecular basis of viral resistance to protease inhibitors. By applying selective pressure in HCV replicon systems or cell-based assays, scientists can observe the development of resistance-associated variants in response to Paritaprevir exposure. Sequencing and phenotypic characterization of these variants provide critical insights into mutation patterns, fitness costs, and cross-resistance profiles, supporting the optimization of combination antiviral regimens and resistance surveillance strategies.
Structure-Activity Relationship (SAR) Analysis: Paritaprevir is often used as a reference molecule in structure-activity relationship studies aimed at optimizing protease inhibitor scaffolds. Its well-characterized interaction with the NS3/4A protease serves as a benchmark for evaluating the impact of chemical modifications on inhibitory potency, selectivity, and pharmacokinetic properties. SAR investigations leveraging this compound facilitate the identification of structural motifs that enhance binding affinity or metabolic stability, thereby accelerating the development of improved antiviral candidates.
Pharmacokinetic and Metabolic Profiling: In preclinical research, Paritaprevir is utilized to assess metabolic pathways, enzyme interactions, and transport mechanisms relevant to DAA pharmacology. Studies employing in vitro microsomal systems, hepatocyte cultures, or recombinant enzymes help delineate the metabolic fate of the compound, including the identification of primary metabolites and pathways of biotransformation. Such profiling is essential for understanding drug-drug interaction potential, optimizing dosing strategies, and predicting in vivo behavior of related antiviral agents.
Analytical Method Development: The distinct chemical structure and physicochemical properties of Paritaprevir make it a suitable standard for developing and validating analytical methods in pharmaceutical and bioanalytical laboratories. It is commonly used to establish high-performance liquid chromatography (HPLC), liquid chromatography-mass spectrometry (LC-MS), and other quantitative assays for the detection and quantification of protease inhibitors in complex biological matrices. These validated methods are crucial for pharmacokinetic studies, quality control of research materials, and the monitoring of compound stability under various experimental conditions.
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