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Antiviral activity of hexapeptides derived from conserved regions of bacterial proteases against HCV NS3 protease

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dc.contributor.author Mushtaq, Amna
dc.contributor.author Ghulam Mustafa
dc.contributor.author Ansari, Tariq Mahmood
dc.contributor.author Shad, Muhammad Aslam
dc.contributor.author Cruz-Reyes, Jorge
dc.contributor.author Jamil, Amer
dc.date.accessioned 2022-10-21T10:36:58Z
dc.date.available 2022-10-21T10:36:58Z
dc.date.issued 2021-01-16
dc.identifier.issn 1011-601X
dc.identifier.uri http://142.54.178.187:9060/xmlui/handle/123456789/13547
dc.description.abstract The main cause of hepatitis C is hepatitis C virus or HCV and for the cure of hepatitis C, NS3/4A protease has been found an important and emerging target. A number of HCV NS3/4A protease inhibitors have been discovered which have shown subsequent reduction in reducing the viral load leading to this infection however they are still undergoing clinical trials for improvement. Bacterial proteases are of great pharmaceutical importance and have a key role in various biological processes and in life cycle of several pathogens. The current study was planned to explore hexapeptides derived from conserved regions of bacterial proteases for their potential in blocking the NS3 protease activity of HCV which would finally inhibit HCV multiplication. For this, a novel protease gene nprB was isolated from a thermophilic bacterium Streptomyces thermovulgaris and bioinformatics analyses were performed. PCR amplification and sequencing of nprB gene indicated an open reading frame of 178 aa (20191.18 Dalton).The peptide GGVHIN was the top ranked with minimum S-score of -17.21) followed by hexapeptides VDAHAN, GVGREA, GALNES and VHINSS with their S-scores of -14.73, -13.78, -10.72 and -10.70, respectively. A phylogram was also reconstructed to reveal evolutionary relationships of nprB with its various homologs. The provided data will serve as a background to further reveal pharmaceutical and biotechnological importance of this novel protease gene from S. thermovulgaris in future. en_US
dc.language.iso en en_US
dc.publisher Karachi: Faculty of Pharmacy & Pharmaceutical Sciecnes, University of Karachi en_US
dc.subject Hepatitis C virus en_US
dc.subject NS3/4A protease en_US
dc.subject molecular docking en_US
dc.subject hexapeptides en_US
dc.subject Streptomyces thermovulgaris en_US
dc.title Antiviral activity of hexapeptides derived from conserved regions of bacterial proteases against HCV NS3 protease en_US
dc.type Article en_US


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