Peptidic inhibitors of the hepatitis C virus serine protease within non-structural protein 3.
New treatments for HCV (Hepatitis C virus) infections are likely to arise from inhibition of the essential, virally-encoded enzymes. These targets include the serine protease required for processing of the HCV polyprotein. The protease constitutes one functional domain of the bifunctional HCV NS3 (non-structural protein 3). Here, insights regarding the NS3 structure and recently synthesized NS3 inhibitors are reviewed. Interestingly, many NS3 protease inhibitors have taken advantage of an unusual product inhibition by N-terminal products of cleavage at the polyprotein processing sites.
D000818:Animals; D016174:Hepacivirus / Q000737:chemistry / Q000187:drug effects / Q000201:enzymology*; D006526:Hepatitis C / Q000188:drug therapy / Q000201:enzymology; D006801:Humans; D010455:Peptides / Q000037:antagonists & inhibitors*; D017434:Protein Structure, Tertiary / Q000187:drug effects; D012697:Serine Endopeptidases / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology*; D017361:Viral Nonstructural Proteins / Q000037:antagonists & inhibitors*; D043583:Nucleoside-Triphosphatase; D053487:DEAD-box RNA Helicases; D000085242:Viral Proteases
D010455:Peptides; D012697:Serine Endopeptidases; D015842:Serine Proteinase Inhibitors; D017361:Viral Nonstructural Proteins; C084422:NS3 protein, hepatitis C virus; D043583:Nucleoside-Triphosphatase; D053487:DEAD-box RNA Helicases; D000085242:Viral Proteases