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3d version 17.3  (DNASTAR)


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    DNASTAR 3d version 17.3
    In silico testing of SARS CoV-2 Delta variant predicts Paradigm’s ACE-2 variant LVE/STR chimera out-scores competing ACE-2 chimeric technologies. Top panel: molecular modeling with Protean 3D Version 17.3 (DNASTAR. Madison, WI) software of ACE-2 LVE construct (green) binding to w.t. SARS-CoV-2 RBD (red) yields DFIRE score = −6.67. Bottom panel: identical modeling of ACE-2 LiVE construct (green) binding to SARS-CoV-2 Delta variant yields DFIRE score = −6.80, slightly tighter (stabilizing) than that for the w.t. RBD. Note rotation of RBD F456 (yellow) in Delta variant toward ACE-2 AA 27, made permissive by the T27L mutation.
    3d Version 17.3, supplied by DNASTAR, used in various techniques. Bioz Stars score: 90/100, based on 62 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/3d version 17.3/product/DNASTAR
    Average 90 stars, based on 62 article reviews
    3d version 17.3 - by Bioz Stars, 2026-04
    90/100 stars

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    1) Product Images from "Design of a chimeric ACE-2/Fc-silent fusion protein with ultrahigh affinity and neutralizing capacity for SARS-CoV-2 variants"

    Article Title: Design of a chimeric ACE-2/Fc-silent fusion protein with ultrahigh affinity and neutralizing capacity for SARS-CoV-2 variants

    Journal: Antibody Therapeutics

    doi: 10.1093/abt/tbad001

    In silico testing of SARS CoV-2 Delta variant predicts Paradigm’s ACE-2 variant LVE/STR chimera out-scores competing ACE-2 chimeric technologies. Top panel: molecular modeling with Protean 3D Version 17.3 (DNASTAR. Madison, WI) software of ACE-2 LVE construct (green) binding to w.t. SARS-CoV-2 RBD (red) yields DFIRE score = −6.67. Bottom panel: identical modeling of ACE-2 LiVE construct (green) binding to SARS-CoV-2 Delta variant yields DFIRE score = −6.80, slightly tighter (stabilizing) than that for the w.t. RBD. Note rotation of RBD F456 (yellow) in Delta variant toward ACE-2 AA 27, made permissive by the T27L mutation.
    Figure Legend Snippet: In silico testing of SARS CoV-2 Delta variant predicts Paradigm’s ACE-2 variant LVE/STR chimera out-scores competing ACE-2 chimeric technologies. Top panel: molecular modeling with Protean 3D Version 17.3 (DNASTAR. Madison, WI) software of ACE-2 LVE construct (green) binding to w.t. SARS-CoV-2 RBD (red) yields DFIRE score = −6.67. Bottom panel: identical modeling of ACE-2 LiVE construct (green) binding to SARS-CoV-2 Delta variant yields DFIRE score = −6.80, slightly tighter (stabilizing) than that for the w.t. RBD. Note rotation of RBD F456 (yellow) in Delta variant toward ACE-2 AA 27, made permissive by the T27L mutation.

    Techniques Used: In Silico, Variant Assay, Software, Construct, Binding Assay, Mutagenesis

    Critical features of Paradigm’s chimeric ACE-2/Fc-silent antibody technology. These include: the use of a full length human ACE-2 domain (AAs 18–740, blue), which when modified as described next, substantially increases binding affinity for SARS CoV-2 RBD/spike protein (green); the choice of specific mutations in ACE-2 (top right red orange, light green AAs) that impart picomolar affinity for the RBD and ~ femtomolar affinity for the full-length spike protein; linkage of the ACE-2 construct to a completely Fc-silent “STR” mutated monoclonal antibody (yellow, Mike Clark PhD, used with permission). The use of STR technology in an ACE2 chimeric prophylactic for SARS CoV-2 is patent pending, see . In addition, one of the two mAb chimeras (“LiVE-Longer” vs. “LiVE”) utilizes a Y-T-E variant (red AAs, bottom) for increased half-life by binding to FcRn, which recycles IgG and is thereby predicted to increase its biological half-life by 3–4-fold (see and text for details). The “LiVE” mAB does not contain the YTE sequence; both LiVE and LiVE-Longer are tested in ( – and ). This figure was generated by Protean 3D, Version 17.3 (DNASTAR. Madison, WI).
    Figure Legend Snippet: Critical features of Paradigm’s chimeric ACE-2/Fc-silent antibody technology. These include: the use of a full length human ACE-2 domain (AAs 18–740, blue), which when modified as described next, substantially increases binding affinity for SARS CoV-2 RBD/spike protein (green); the choice of specific mutations in ACE-2 (top right red orange, light green AAs) that impart picomolar affinity for the RBD and ~ femtomolar affinity for the full-length spike protein; linkage of the ACE-2 construct to a completely Fc-silent “STR” mutated monoclonal antibody (yellow, Mike Clark PhD, used with permission). The use of STR technology in an ACE2 chimeric prophylactic for SARS CoV-2 is patent pending, see . In addition, one of the two mAb chimeras (“LiVE-Longer” vs. “LiVE”) utilizes a Y-T-E variant (red AAs, bottom) for increased half-life by binding to FcRn, which recycles IgG and is thereby predicted to increase its biological half-life by 3–4-fold (see and text for details). The “LiVE” mAB does not contain the YTE sequence; both LiVE and LiVE-Longer are tested in ( – and ). This figure was generated by Protean 3D, Version 17.3 (DNASTAR. Madison, WI).

    Techniques Used: Modification, Binding Assay, Construct, Variant Assay, Sequencing, Generated

    The designed ACE-2 variant LVE/STR chimera scores higher than other ACE-2 Fusion protein competitors by the DFIRE scoring method. Molecular modeling was conducted with Protean 3D Version 17.3 (DNASTAR. Madison, WI) software, aimed at testing Paradigms’ proprietary LiVE variant (ACE-2 mutations T27L, H34V, and N90E) binding to w.t. SARS-2 RBD (DFIRE = −6.67), as it compares to the ACE-2 variant YTY (ACE-2 mutations T27Y, L79T and N330Y) binding to the w.t. SARS-2 RBD (DFIRE = −4.53). A lower DFIRE score predicts tighter (stabilizing) protein–protein interactions. See Methods for details.
    Figure Legend Snippet: The designed ACE-2 variant LVE/STR chimera scores higher than other ACE-2 Fusion protein competitors by the DFIRE scoring method. Molecular modeling was conducted with Protean 3D Version 17.3 (DNASTAR. Madison, WI) software, aimed at testing Paradigms’ proprietary LiVE variant (ACE-2 mutations T27L, H34V, and N90E) binding to w.t. SARS-2 RBD (DFIRE = −6.67), as it compares to the ACE-2 variant YTY (ACE-2 mutations T27Y, L79T and N330Y) binding to the w.t. SARS-2 RBD (DFIRE = −4.53). A lower DFIRE score predicts tighter (stabilizing) protein–protein interactions. See Methods for details.

    Techniques Used: Variant Assay, Software, Binding Assay



    Similar Products

    3d version 17.3  (DNASTAR)
    90
    DNASTAR 3d version 17.3
    In silico testing of SARS CoV-2 Delta variant predicts Paradigm’s ACE-2 variant LVE/STR chimera out-scores competing ACE-2 chimeric technologies. Top panel: molecular modeling with Protean 3D Version 17.3 (DNASTAR. Madison, WI) software of ACE-2 LVE construct (green) binding to w.t. SARS-CoV-2 RBD (red) yields DFIRE score = −6.67. Bottom panel: identical modeling of ACE-2 LiVE construct (green) binding to SARS-CoV-2 Delta variant yields DFIRE score = −6.80, slightly tighter (stabilizing) than that for the w.t. RBD. Note rotation of RBD F456 (yellow) in Delta variant toward ACE-2 AA 27, made permissive by the T27L mutation.
    3d Version 17.3, supplied by DNASTAR, 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/result/3d version 17.3/product/DNASTAR
    Average 90 stars, based on 1 article reviews
    3d version 17.3 - by Bioz Stars, 2026-04
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    In silico testing of SARS CoV-2 Delta variant predicts Paradigm’s ACE-2 variant LVE/STR chimera out-scores competing ACE-2 chimeric technologies. Top panel: molecular modeling with Protean 3D Version 17.3 (DNASTAR. Madison, WI) software of ACE-2 LVE construct (green) binding to w.t. SARS-CoV-2 RBD (red) yields DFIRE score = −6.67. Bottom panel: identical modeling of ACE-2 LiVE construct (green) binding to SARS-CoV-2 Delta variant yields DFIRE score = −6.80, slightly tighter (stabilizing) than that for the w.t. RBD. Note rotation of RBD F456 (yellow) in Delta variant toward ACE-2 AA 27, made permissive by the T27L mutation.

    Journal: Antibody Therapeutics

    Article Title: Design of a chimeric ACE-2/Fc-silent fusion protein with ultrahigh affinity and neutralizing capacity for SARS-CoV-2 variants

    doi: 10.1093/abt/tbad001

    Figure Lengend Snippet: In silico testing of SARS CoV-2 Delta variant predicts Paradigm’s ACE-2 variant LVE/STR chimera out-scores competing ACE-2 chimeric technologies. Top panel: molecular modeling with Protean 3D Version 17.3 (DNASTAR. Madison, WI) software of ACE-2 LVE construct (green) binding to w.t. SARS-CoV-2 RBD (red) yields DFIRE score = −6.67. Bottom panel: identical modeling of ACE-2 LiVE construct (green) binding to SARS-CoV-2 Delta variant yields DFIRE score = −6.80, slightly tighter (stabilizing) than that for the w.t. RBD. Note rotation of RBD F456 (yellow) in Delta variant toward ACE-2 AA 27, made permissive by the T27L mutation.

    Article Snippet: Molecular models were derived from publicly available ACE-2 and SARS-CoV-2 sequence databases ( Outbreak.info ) with Protean 3D Version 17.3 (DNASTAR.

    Techniques: In Silico, Variant Assay, Software, Construct, Binding Assay, Mutagenesis

    Critical features of Paradigm’s chimeric ACE-2/Fc-silent antibody technology. These include: the use of a full length human ACE-2 domain (AAs 18–740, blue), which when modified as described next, substantially increases binding affinity for SARS CoV-2 RBD/spike protein (green); the choice of specific mutations in ACE-2 (top right red orange, light green AAs) that impart picomolar affinity for the RBD and ~ femtomolar affinity for the full-length spike protein; linkage of the ACE-2 construct to a completely Fc-silent “STR” mutated monoclonal antibody (yellow, Mike Clark PhD, used with permission). The use of STR technology in an ACE2 chimeric prophylactic for SARS CoV-2 is patent pending, see . In addition, one of the two mAb chimeras (“LiVE-Longer” vs. “LiVE”) utilizes a Y-T-E variant (red AAs, bottom) for increased half-life by binding to FcRn, which recycles IgG and is thereby predicted to increase its biological half-life by 3–4-fold (see and text for details). The “LiVE” mAB does not contain the YTE sequence; both LiVE and LiVE-Longer are tested in ( – and ). This figure was generated by Protean 3D, Version 17.3 (DNASTAR. Madison, WI).

    Journal: Antibody Therapeutics

    Article Title: Design of a chimeric ACE-2/Fc-silent fusion protein with ultrahigh affinity and neutralizing capacity for SARS-CoV-2 variants

    doi: 10.1093/abt/tbad001

    Figure Lengend Snippet: Critical features of Paradigm’s chimeric ACE-2/Fc-silent antibody technology. These include: the use of a full length human ACE-2 domain (AAs 18–740, blue), which when modified as described next, substantially increases binding affinity for SARS CoV-2 RBD/spike protein (green); the choice of specific mutations in ACE-2 (top right red orange, light green AAs) that impart picomolar affinity for the RBD and ~ femtomolar affinity for the full-length spike protein; linkage of the ACE-2 construct to a completely Fc-silent “STR” mutated monoclonal antibody (yellow, Mike Clark PhD, used with permission). The use of STR technology in an ACE2 chimeric prophylactic for SARS CoV-2 is patent pending, see . In addition, one of the two mAb chimeras (“LiVE-Longer” vs. “LiVE”) utilizes a Y-T-E variant (red AAs, bottom) for increased half-life by binding to FcRn, which recycles IgG and is thereby predicted to increase its biological half-life by 3–4-fold (see and text for details). The “LiVE” mAB does not contain the YTE sequence; both LiVE and LiVE-Longer are tested in ( – and ). This figure was generated by Protean 3D, Version 17.3 (DNASTAR. Madison, WI).

    Article Snippet: Molecular models were derived from publicly available ACE-2 and SARS-CoV-2 sequence databases ( Outbreak.info ) with Protean 3D Version 17.3 (DNASTAR.

    Techniques: Modification, Binding Assay, Construct, Variant Assay, Sequencing, Generated

    The designed ACE-2 variant LVE/STR chimera scores higher than other ACE-2 Fusion protein competitors by the DFIRE scoring method. Molecular modeling was conducted with Protean 3D Version 17.3 (DNASTAR. Madison, WI) software, aimed at testing Paradigms’ proprietary LiVE variant (ACE-2 mutations T27L, H34V, and N90E) binding to w.t. SARS-2 RBD (DFIRE = −6.67), as it compares to the ACE-2 variant YTY (ACE-2 mutations T27Y, L79T and N330Y) binding to the w.t. SARS-2 RBD (DFIRE = −4.53). A lower DFIRE score predicts tighter (stabilizing) protein–protein interactions. See Methods for details.

    Journal: Antibody Therapeutics

    Article Title: Design of a chimeric ACE-2/Fc-silent fusion protein with ultrahigh affinity and neutralizing capacity for SARS-CoV-2 variants

    doi: 10.1093/abt/tbad001

    Figure Lengend Snippet: The designed ACE-2 variant LVE/STR chimera scores higher than other ACE-2 Fusion protein competitors by the DFIRE scoring method. Molecular modeling was conducted with Protean 3D Version 17.3 (DNASTAR. Madison, WI) software, aimed at testing Paradigms’ proprietary LiVE variant (ACE-2 mutations T27L, H34V, and N90E) binding to w.t. SARS-2 RBD (DFIRE = −6.67), as it compares to the ACE-2 variant YTY (ACE-2 mutations T27Y, L79T and N330Y) binding to the w.t. SARS-2 RBD (DFIRE = −4.53). A lower DFIRE score predicts tighter (stabilizing) protein–protein interactions. See Methods for details.

    Article Snippet: Molecular models were derived from publicly available ACE-2 and SARS-CoV-2 sequence databases ( Outbreak.info ) with Protean 3D Version 17.3 (DNASTAR.

    Techniques: Variant Assay, Software, Binding Assay