The Experts below are selected from a list of 3 Experts worldwide ranked by ideXlab platform
Peter W. Bergum - One of the best experts on this subject based on the ideXlab platform.
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Optimization of a continuous assay for obtaining sensitive kinetic data on the inhibition of the HCV NS3 protease
Peptides for the New Millennium, 2020Co-Authors: Marguerita Lim-wilby, Susanne M Anderson, John Gaudette, Odile Esther Levy, Thomas G. Nolan, Peter W. BergumAbstract:Hepatitis C, which is caused by HCV, affects about 2% of the world’s population and is responsible for more than 50 million cases of hepatocellular carcinomas worldwide. HCV uses Hepacivirin, a serine protease at the N-terminal third of the protein product of its NS3 gene, to process its NS4a-NS4b-NS5a-NS5b polyprotein. In addition, Hepacivirin cleaves internally the NS3-NS4a site, releasing its cofactor NS4a. Inhibition of Hepacivirin’s activity is one strategy for developing drugs to treat hepatitis C. Methods to measure the activity and inhibition of Hepacivirin have included the use of polyproteins, peptides, and depsipeptides as substrates in PAGE, ELISA, BIAcore, and RP-HPLC-based assays [1-5]. More preferable are continuous chromogenic and fluorogenic assays, which use commercially available peptide-pNAs and peptide-AMCs, respectively. Additionally, an assay using peptide-p-phenylazophenyl ester as substrate has been developed [6], which is limiting due to a requirement for low pH and inherent high background and stability problems. Most recently, a continuous assay based on fluorescence resonance energy transfer (FRET) depsipeptide substrates has been presented [7]. Using the same FRET principle, we designed depsipeptide substrates for greater ease of chemical synthesis, lower molecular weight, and enhancing assay sensitivity with lower background, while maintaining the advantages of compatibility and stability at physiologic pH.
Marguerita Lim-wilby - One of the best experts on this subject based on the ideXlab platform.
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Optimization of a continuous assay for obtaining sensitive kinetic data on the inhibition of the HCV NS3 protease
Peptides for the New Millennium, 2020Co-Authors: Marguerita Lim-wilby, Susanne M Anderson, John Gaudette, Odile Esther Levy, Thomas G. Nolan, Peter W. BergumAbstract:Hepatitis C, which is caused by HCV, affects about 2% of the world’s population and is responsible for more than 50 million cases of hepatocellular carcinomas worldwide. HCV uses Hepacivirin, a serine protease at the N-terminal third of the protein product of its NS3 gene, to process its NS4a-NS4b-NS5a-NS5b polyprotein. In addition, Hepacivirin cleaves internally the NS3-NS4a site, releasing its cofactor NS4a. Inhibition of Hepacivirin’s activity is one strategy for developing drugs to treat hepatitis C. Methods to measure the activity and inhibition of Hepacivirin have included the use of polyproteins, peptides, and depsipeptides as substrates in PAGE, ELISA, BIAcore, and RP-HPLC-based assays [1-5]. More preferable are continuous chromogenic and fluorogenic assays, which use commercially available peptide-pNAs and peptide-AMCs, respectively. Additionally, an assay using peptide-p-phenylazophenyl ester as substrate has been developed [6], which is limiting due to a requirement for low pH and inherent high background and stability problems. Most recently, a continuous assay based on fluorescence resonance energy transfer (FRET) depsipeptide substrates has been presented [7]. Using the same FRET principle, we designed depsipeptide substrates for greater ease of chemical synthesis, lower molecular weight, and enhancing assay sensitivity with lower background, while maintaining the advantages of compatibility and stability at physiologic pH.
Susanne M Anderson - One of the best experts on this subject based on the ideXlab platform.
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Optimization of a continuous assay for obtaining sensitive kinetic data on the inhibition of the HCV NS3 protease
Peptides for the New Millennium, 2020Co-Authors: Marguerita Lim-wilby, Susanne M Anderson, John Gaudette, Odile Esther Levy, Thomas G. Nolan, Peter W. BergumAbstract:Hepatitis C, which is caused by HCV, affects about 2% of the world’s population and is responsible for more than 50 million cases of hepatocellular carcinomas worldwide. HCV uses Hepacivirin, a serine protease at the N-terminal third of the protein product of its NS3 gene, to process its NS4a-NS4b-NS5a-NS5b polyprotein. In addition, Hepacivirin cleaves internally the NS3-NS4a site, releasing its cofactor NS4a. Inhibition of Hepacivirin’s activity is one strategy for developing drugs to treat hepatitis C. Methods to measure the activity and inhibition of Hepacivirin have included the use of polyproteins, peptides, and depsipeptides as substrates in PAGE, ELISA, BIAcore, and RP-HPLC-based assays [1-5]. More preferable are continuous chromogenic and fluorogenic assays, which use commercially available peptide-pNAs and peptide-AMCs, respectively. Additionally, an assay using peptide-p-phenylazophenyl ester as substrate has been developed [6], which is limiting due to a requirement for low pH and inherent high background and stability problems. Most recently, a continuous assay based on fluorescence resonance energy transfer (FRET) depsipeptide substrates has been presented [7]. Using the same FRET principle, we designed depsipeptide substrates for greater ease of chemical synthesis, lower molecular weight, and enhancing assay sensitivity with lower background, while maintaining the advantages of compatibility and stability at physiologic pH.
John Gaudette - One of the best experts on this subject based on the ideXlab platform.
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Optimization of a continuous assay for obtaining sensitive kinetic data on the inhibition of the HCV NS3 protease
Peptides for the New Millennium, 2020Co-Authors: Marguerita Lim-wilby, Susanne M Anderson, John Gaudette, Odile Esther Levy, Thomas G. Nolan, Peter W. BergumAbstract:Hepatitis C, which is caused by HCV, affects about 2% of the world’s population and is responsible for more than 50 million cases of hepatocellular carcinomas worldwide. HCV uses Hepacivirin, a serine protease at the N-terminal third of the protein product of its NS3 gene, to process its NS4a-NS4b-NS5a-NS5b polyprotein. In addition, Hepacivirin cleaves internally the NS3-NS4a site, releasing its cofactor NS4a. Inhibition of Hepacivirin’s activity is one strategy for developing drugs to treat hepatitis C. Methods to measure the activity and inhibition of Hepacivirin have included the use of polyproteins, peptides, and depsipeptides as substrates in PAGE, ELISA, BIAcore, and RP-HPLC-based assays [1-5]. More preferable are continuous chromogenic and fluorogenic assays, which use commercially available peptide-pNAs and peptide-AMCs, respectively. Additionally, an assay using peptide-p-phenylazophenyl ester as substrate has been developed [6], which is limiting due to a requirement for low pH and inherent high background and stability problems. Most recently, a continuous assay based on fluorescence resonance energy transfer (FRET) depsipeptide substrates has been presented [7]. Using the same FRET principle, we designed depsipeptide substrates for greater ease of chemical synthesis, lower molecular weight, and enhancing assay sensitivity with lower background, while maintaining the advantages of compatibility and stability at physiologic pH.
Odile Esther Levy - One of the best experts on this subject based on the ideXlab platform.
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Optimization of a continuous assay for obtaining sensitive kinetic data on the inhibition of the HCV NS3 protease
Peptides for the New Millennium, 2020Co-Authors: Marguerita Lim-wilby, Susanne M Anderson, John Gaudette, Odile Esther Levy, Thomas G. Nolan, Peter W. BergumAbstract:Hepatitis C, which is caused by HCV, affects about 2% of the world’s population and is responsible for more than 50 million cases of hepatocellular carcinomas worldwide. HCV uses Hepacivirin, a serine protease at the N-terminal third of the protein product of its NS3 gene, to process its NS4a-NS4b-NS5a-NS5b polyprotein. In addition, Hepacivirin cleaves internally the NS3-NS4a site, releasing its cofactor NS4a. Inhibition of Hepacivirin’s activity is one strategy for developing drugs to treat hepatitis C. Methods to measure the activity and inhibition of Hepacivirin have included the use of polyproteins, peptides, and depsipeptides as substrates in PAGE, ELISA, BIAcore, and RP-HPLC-based assays [1-5]. More preferable are continuous chromogenic and fluorogenic assays, which use commercially available peptide-pNAs and peptide-AMCs, respectively. Additionally, an assay using peptide-p-phenylazophenyl ester as substrate has been developed [6], which is limiting due to a requirement for low pH and inherent high background and stability problems. Most recently, a continuous assay based on fluorescence resonance energy transfer (FRET) depsipeptide substrates has been presented [7]. Using the same FRET principle, we designed depsipeptide substrates for greater ease of chemical synthesis, lower molecular weight, and enhancing assay sensitivity with lower background, while maintaining the advantages of compatibility and stability at physiologic pH.