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lineweaver–burk plot and global data fitting for competitive inhibition  (GraphPad Software Inc)


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    GraphPad Software Inc lineweaver–burk plot and global data fitting for competitive inhibition
    3CL protease inhibitors for SARS-CoV-1 with electrophilic arylketone warhead. (A) Structures of 3CL pro inhibitors 1 , SH-5, YH-53, and YH-71. SH-5 contains a tripeptide scaffold with a warhead and a carbamoyl unit at P4. YH-53 and YH-71 consist of a dipeptide scaffold with a warhead and a heteroaromatic unit at P3. (B) Proposed mechanism of <t>inhibition</t> by SH-5. Once SH-5 is bound to the enzyme, the active site Cys145 of 3CL pro attacks the ketone of SH-5 to afford a reversible covalent bond. The hemithioketal intermediate would then be stabilized by an oxyanion hole.
    Lineweaver–Burk Plot And Global Data Fitting For Competitive Inhibition, supplied by GraphPad Software Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/lineweaver%E2%80%93burk+plot+and+global+data+fitting+for+competitive+inhibition/pmc08340582-183-9-14?v=GraphPad+Software+Inc
    Average 90 stars, based on 1 article reviews
    lineweaver–burk plot and global data fitting for competitive inhibition - by Bioz Stars, 2026-07
    90/100 stars

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    1) Product Images from "3CL Protease Inhibitors with an Electrophilic Arylketone Moiety as Anti-SARS-CoV-2 Agents"

    Article Title: 3CL Protease Inhibitors with an Electrophilic Arylketone Moiety as Anti-SARS-CoV-2 Agents

    Journal: Journal of Medicinal Chemistry

    doi: 10.1021/acs.jmedchem.1c00665

    3CL protease inhibitors for SARS-CoV-1 with electrophilic arylketone warhead. (A) Structures of 3CL pro inhibitors 1 , SH-5, YH-53, and YH-71. SH-5 contains a tripeptide scaffold with a warhead and a carbamoyl unit at P4. YH-53 and YH-71 consist of a dipeptide scaffold with a warhead and a heteroaromatic unit at P3. (B) Proposed mechanism of inhibition by SH-5. Once SH-5 is bound to the enzyme, the active site Cys145 of 3CL pro attacks the ketone of SH-5 to afford a reversible covalent bond. The hemithioketal intermediate would then be stabilized by an oxyanion hole.
    Figure Legend Snippet: 3CL protease inhibitors for SARS-CoV-1 with electrophilic arylketone warhead. (A) Structures of 3CL pro inhibitors 1 , SH-5, YH-53, and YH-71. SH-5 contains a tripeptide scaffold with a warhead and a carbamoyl unit at P4. YH-53 and YH-71 consist of a dipeptide scaffold with a warhead and a heteroaromatic unit at P3. (B) Proposed mechanism of inhibition by SH-5. Once SH-5 is bound to the enzyme, the active site Cys145 of 3CL pro attacks the ketone of SH-5 to afford a reversible covalent bond. The hemithioketal intermediate would then be stabilized by an oxyanion hole.

    Techniques Used: Inhibition

    SARS-CoV-2 3CL pro inhibitory assay. (A) Concentration-dependent inhibition of SARS-CoV-2 3CL pro by SH-5, YH-53 and YH-71. Reactions were monitored for 10 min. Data points represent mean values ± SEM from three independent experiments. K i values were calculated using the Cheng–Prusoff equation and are noted in Figure . The K m value of the substrate was 48.4 μM. (B) Lineweaver–Burk plot for SH-5 inhibition of SARS-CoV-2 3CL pro at 15, 30, 45, 60, and 75 μM of fluorogenic substrate and 0, 10, 20, 30, 40, and 50 nM of the inhibitor SH-5. Three independent experiments were performed, and reactions were monitored for 10 min. The common intercept on the ordinate indicates a competitive inhibition type. (C) Global fit of kinetic data from (B) for competitive enzyme inhibition. The best fit value of K i 19.8 ± 2.3 nM was in the same range as the value calculated by the Cheng–Prusoff equation (see Figure ).
    Figure Legend Snippet: SARS-CoV-2 3CL pro inhibitory assay. (A) Concentration-dependent inhibition of SARS-CoV-2 3CL pro by SH-5, YH-53 and YH-71. Reactions were monitored for 10 min. Data points represent mean values ± SEM from three independent experiments. K i values were calculated using the Cheng–Prusoff equation and are noted in Figure . The K m value of the substrate was 48.4 μM. (B) Lineweaver–Burk plot for SH-5 inhibition of SARS-CoV-2 3CL pro at 15, 30, 45, 60, and 75 μM of fluorogenic substrate and 0, 10, 20, 30, 40, and 50 nM of the inhibitor SH-5. Three independent experiments were performed, and reactions were monitored for 10 min. The common intercept on the ordinate indicates a competitive inhibition type. (C) Global fit of kinetic data from (B) for competitive enzyme inhibition. The best fit value of K i 19.8 ± 2.3 nM was in the same range as the value calculated by the Cheng–Prusoff equation (see Figure ).

    Techniques Used: Concentration Assay, Inhibition, Enzyme Inhibition Assay



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    lineweaver–burk plot and global data fitting for competitive inhibition  (GraphPad Software Inc)
    90
    GraphPad Software Inc lineweaver–burk plot and global data fitting for competitive inhibition
    3CL protease inhibitors for SARS-CoV-1 with electrophilic arylketone warhead. (A) Structures of 3CL pro inhibitors 1 , SH-5, YH-53, and YH-71. SH-5 contains a tripeptide scaffold with a warhead and a carbamoyl unit at P4. YH-53 and YH-71 consist of a dipeptide scaffold with a warhead and a heteroaromatic unit at P3. (B) Proposed mechanism of <t>inhibition</t> by SH-5. Once SH-5 is bound to the enzyme, the active site Cys145 of 3CL pro attacks the ketone of SH-5 to afford a reversible covalent bond. The hemithioketal intermediate would then be stabilized by an oxyanion hole.
    Lineweaver–Burk Plot And Global Data Fitting For Competitive Inhibition, supplied by GraphPad Software Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/lineweaver%E2%80%93burk+plot+and+global+data+fitting+for+competitive+inhibition/pmc08340582-183-9-14?v=GraphPad+Software+Inc
    Average 90 stars, based on 1 article reviews
    lineweaver–burk plot and global data fitting for competitive inhibition - by Bioz Stars, 2026-07
    90/100 stars
    		  Buy from Supplier

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    3CL protease inhibitors for SARS-CoV-1 with electrophilic arylketone warhead. (A) Structures of 3CL pro inhibitors 1 , SH-5, YH-53, and YH-71. SH-5 contains a tripeptide scaffold with a warhead and a carbamoyl unit at P4. YH-53 and YH-71 consist of a dipeptide scaffold with a warhead and a heteroaromatic unit at P3. (B) Proposed mechanism of inhibition by SH-5. Once SH-5 is bound to the enzyme, the active site Cys145 of 3CL pro attacks the ketone of SH-5 to afford a reversible covalent bond. The hemithioketal intermediate would then be stabilized by an oxyanion hole.

    Journal: Journal of Medicinal Chemistry

    Article Title: 3CL Protease Inhibitors with an Electrophilic Arylketone Moiety as Anti-SARS-CoV-2 Agents

    doi: 10.1021/acs.jmedchem.1c00665

    Figure Lengend Snippet: 3CL protease inhibitors for SARS-CoV-1 with electrophilic arylketone warhead. (A) Structures of 3CL pro inhibitors 1 , SH-5, YH-53, and YH-71. SH-5 contains a tripeptide scaffold with a warhead and a carbamoyl unit at P4. YH-53 and YH-71 consist of a dipeptide scaffold with a warhead and a heteroaromatic unit at P3. (B) Proposed mechanism of inhibition by SH-5. Once SH-5 is bound to the enzyme, the active site Cys145 of 3CL pro attacks the ketone of SH-5 to afford a reversible covalent bond. The hemithioketal intermediate would then be stabilized by an oxyanion hole.

    Article Snippet: The Lineweaver–Burk plot and the global data fitting for competitive inhibition were performed with GraphPad Prism 8.0.

    Techniques: Inhibition

    SARS-CoV-2 3CL pro inhibitory assay. (A) Concentration-dependent inhibition of SARS-CoV-2 3CL pro by SH-5, YH-53 and YH-71. Reactions were monitored for 10 min. Data points represent mean values ± SEM from three independent experiments. K i values were calculated using the Cheng–Prusoff equation and are noted in Figure . The K m value of the substrate was 48.4 μM. (B) Lineweaver–Burk plot for SH-5 inhibition of SARS-CoV-2 3CL pro at 15, 30, 45, 60, and 75 μM of fluorogenic substrate and 0, 10, 20, 30, 40, and 50 nM of the inhibitor SH-5. Three independent experiments were performed, and reactions were monitored for 10 min. The common intercept on the ordinate indicates a competitive inhibition type. (C) Global fit of kinetic data from (B) for competitive enzyme inhibition. The best fit value of K i 19.8 ± 2.3 nM was in the same range as the value calculated by the Cheng–Prusoff equation (see Figure ).

    Journal: Journal of Medicinal Chemistry

    Article Title: 3CL Protease Inhibitors with an Electrophilic Arylketone Moiety as Anti-SARS-CoV-2 Agents

    doi: 10.1021/acs.jmedchem.1c00665

    Figure Lengend Snippet: SARS-CoV-2 3CL pro inhibitory assay. (A) Concentration-dependent inhibition of SARS-CoV-2 3CL pro by SH-5, YH-53 and YH-71. Reactions were monitored for 10 min. Data points represent mean values ± SEM from three independent experiments. K i values were calculated using the Cheng–Prusoff equation and are noted in Figure . The K m value of the substrate was 48.4 μM. (B) Lineweaver–Burk plot for SH-5 inhibition of SARS-CoV-2 3CL pro at 15, 30, 45, 60, and 75 μM of fluorogenic substrate and 0, 10, 20, 30, 40, and 50 nM of the inhibitor SH-5. Three independent experiments were performed, and reactions were monitored for 10 min. The common intercept on the ordinate indicates a competitive inhibition type. (C) Global fit of kinetic data from (B) for competitive enzyme inhibition. The best fit value of K i 19.8 ± 2.3 nM was in the same range as the value calculated by the Cheng–Prusoff equation (see Figure ).

    Article Snippet: The Lineweaver–Burk plot and the global data fitting for competitive inhibition were performed with GraphPad Prism 8.0.

    Techniques: Concentration Assay, Inhibition, Enzyme Inhibition Assay