By Kuo-Chen Chou, Dong-Qing Wei, Qi-Shi Du (auth.), Uwe Lendeckel, Nigel M. Hooper (eds.)
The 8th quantity within the Proteases in Biology and disorder sequence specializes in the function of proteases in virus functionality and their capability as anti-viral objectives. Viral infections are nonetheless tough to hazard and a few remained life-threatening illnesses inspite of antiviral drug examine over many years. Proteases are nonetheless considered as an Achilles’ heel of the pathogens and, therefore, protease inhibitors can help to address the identified and the rising viral threads. The e-book discusses viral proteases of an important pathogenic viruses, accountable for critical ailments: AIDS, SARS, Hepatitis, Cytomegalovirus, T-cell lymphotropic virus, Picornavirus. This ebook focuses particularly at the viral proteases, the most important necessities for viral access into cells and viral replication. Viral proteases signify a tremendous pharmaceutical goal. the present level of protease inhibitor improvement and treatment are summarised and mentioned via specialists within the box. This quantity represents a well timed and helpful continuation of the Proteases in Biology and sickness sequence. The reader will examine the opportunity of proteases as goals for powerful anti-virals. This publication may be a worthwhile resource of data on viral proteases and galvanize additional examine during this vital field.
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Additional resources for Viral Proteases and Antiviral Protease Inhibitor Therapy: Proteases in Biology and Disease
T. Weber et al. replication so that no infectious virus can be produced. Consequently, inhibitors of HIV-1 protease are effective antiviral agents for AIDS therapy. In addition, the polyprotein substrate of the protease has become a new target for antiviral agents. A novel antiviral inhibitor of maturation is in clinical trials. , 2003). Other maturation inhibitors can be designed on the same principle to block maturation by binding to other critical cleavage sites. The majority of clinical antiviral inhibitors, however, bind in the protease active site and were designed with knowledge of the HIV-1 protease structure and substrate specificity.
Also, how to modify these octapeptides and make them become potent inhibitors is suggested. Finally, a step-to-step guide on how to use ProtIdent, a web server for identifying proteases and their types (Chou and Shen, 2008), is presented that may be useful for people working in the area of Proteases in Biology and Disease. -C. Chou et al. References Adessi, C. and Soto, C. 2002, Converting a peptide into a drug: strategies to improve stability and bioavailability. Curr Med Chem, 9, 963–978. R. and Hilgenfeld, R.
Peptides, 27, 622–625. X. T. 2003, Prediction for proteinase cleavage sites in polyproteins of coronaviruses and its applications in analyzing SARS-CoV genomes. FEBS Letters, 553, 451–456. D. C. 2006, A novel fingerprint map for detecting SARS-CoV. J Pharmaceut Biomed Analysis, 41, 246–250. X. C. 2007, Agaritine and its derivatives are potential inhibitors against HIV proteases. Med Chem, 3, 221–226. Q. C. 2009, Binding mechanism of H5N1 influenza virus neuraminidase with ligands and its implication for drug design.