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gosilico chromatography modeling software  (Cytiva Europe)


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    Cytiva Europe gosilico chromatography modeling software
    Gosilico Chromatography Modeling Software, supplied by Cytiva Europe, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/modeling+software+package/GoSilico+chromatography+modeling+software+-+Standard+license+package+36+months/pm42834531-109-10-14
    Average 94 stars, based on 2 article reviews
    gosilico chromatography modeling software - by Bioz Stars, 2026-10
    94/100 stars

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    Related Articles

    Chromatography:

    Article Title: Comparative evaluation and simplification of steric mass action and colloidal particle adsorption models for protein ion exchange chromatography
    Article Snippet: Mechanistic modeling of ion exchange chromatography (IEC) has become an essential tool for accelerating process development and deepening mechanistic insight in biopharmaceutical manufacturing.. Although the steric mass action (SMA) model is widely used, it frequently fails to accurately describe elution behavior under high protein loading conditions, whereas the colloidal particle adsorption (CPA) model remains robust.. To clarify the mechanistic advantages of the CPA framework, this study systematically compared the SMA and CPA models for describing the separation of a monoclonal antibody monomer-dimer mixture in IEC.

    Article Title: Development and application of a mechanistic model for protein A resolution of a bispecific antibody for process characterization and optimization.
    Article Snippet: .. Simulations and model quality analysis (Section 3.5) were performed using GoSilico Chromatography Modeling Software (Cytiva) version 1.16.0. ..

    Software:

    Article Title: Comparative evaluation and simplification of steric mass action and colloidal particle adsorption models for protein ion exchange chromatography
    Article Snippet: Mechanistic modeling of ion exchange chromatography (IEC) has become an essential tool for accelerating process development and deepening mechanistic insight in biopharmaceutical manufacturing.. Although the steric mass action (SMA) model is widely used, it frequently fails to accurately describe elution behavior under high protein loading conditions, whereas the colloidal particle adsorption (CPA) model remains robust.. To clarify the mechanistic advantages of the CPA framework, this study systematically compared the SMA and CPA models for describing the separation of a monoclonal antibody monomer-dimer mixture in IEC.

    Article Title: Development and application of a mechanistic model for protein A resolution of a bispecific antibody for process characterization and optimization.
    Article Snippet: .. Simulations and model quality analysis (Section 3.5) were performed using GoSilico Chromatography Modeling Software (Cytiva) version 1.16.0. ..

    Analysis:

    Article Title: Development and application of a mechanistic model for protein A resolution of a bispecific antibody for process characterization and optimization.
    Article Snippet: .. Simulations and model quality analysis (Section 3.5) were performed using GoSilico Chromatography Modeling Software (Cytiva) version 1.16.0. ..



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    Image Search Results


    AlphaFold3 models of TNFR1-ICM11 complexes (A) Native TNFR1–TNF reference structure for epitope orientation (adapted from PDB: 1TNR ). The following contact residues defines TNF binding site: Lys18, Ser49, His52, Trp93, Glu95, Arg132, Lys143, Lys144, Glu42, Ser43, His55, Cys56, Cys59, Ser60, Lys61, Arg63, Lys64, Glu65, and Met66. (B–D) AF3 models for 1:1, 2×, and 3× TNFR1-ICM11 assemblies. The AF3 confidences are indicated in the figure: ipTM provides confidence in the interface quality, and pTM summarizes the overall complex topology. The resulting contact residues of the 1:1 complex are: Arg63, Glu65, His91, Tyr92, Trp93, Glu95, Asn96, Gln99, Phe101, Lys118, Arg132, Glu133, Glu135, Glu147, and Lys150. Shared TNFR1 hotspot residues shared by both TNF and ICM11: Arg63, Glu65, Trp93, Glu95, Arg132. Interface/contact residues were computed via Molecular Operating Environment (MOE) software.

    Journal: iScience

    Article Title: Antigen-directed single domain antibody-based TNFR1 agonists elicit preferential killing of HER2-overexpressing cancer cells

    doi: 10.1016/j.isci.2026.115327

    Figure Lengend Snippet: AlphaFold3 models of TNFR1-ICM11 complexes (A) Native TNFR1–TNF reference structure for epitope orientation (adapted from PDB: 1TNR ). The following contact residues defines TNF binding site: Lys18, Ser49, His52, Trp93, Glu95, Arg132, Lys143, Lys144, Glu42, Ser43, His55, Cys56, Cys59, Ser60, Lys61, Arg63, Lys64, Glu65, and Met66. (B–D) AF3 models for 1:1, 2×, and 3× TNFR1-ICM11 assemblies. The AF3 confidences are indicated in the figure: ipTM provides confidence in the interface quality, and pTM summarizes the overall complex topology. The resulting contact residues of the 1:1 complex are: Arg63, Glu65, His91, Tyr92, Trp93, Glu95, Asn96, Gln99, Phe101, Lys118, Arg132, Glu133, Glu135, Glu147, and Lys150. Shared TNFR1 hotspot residues shared by both TNF and ICM11: Arg63, Glu65, Trp93, Glu95, Arg132. Interface/contact residues were computed via Molecular Operating Environment (MOE) software.

    Article Snippet: molecular modeling software package MOE (Molecular Operating Environment) , Chemical Computing Group Inc. , RRID: SCR_014882.

    Techniques: Binding Assay, Software