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• W1982386830 abstract "Having a theoretical understanding of the orientation of immunoglobulin on an immobilized solid surface is important in biomedical pathogen-detecting systems and cellular analysis. Despite the stable adsorption of immunoglobulin on a polystyrene (PS) surface that has been applied in many kinds of immunoassays, there are many uncertainties in antibody-based clinical and biological experimental methods. To understand the binding mechanism and physicochemical interactions between immunoglobulin and the PS surface at the atomic level, we investigated the binding behavior and interactions of the monoclonal immunoglobulin G (IgG) on the PS surface using the computational method. In our docking simulation with the different arrangement of translational and rotational orientation of IgG onto the PS surface, three typical orientation patterns of the immunoglobulin G on the PS surface were found. We precisely analyzed these orientation patterns and clarified how the immunoglobulin G interacts with the PS surface at atomic scale in the beginning of the adsorption process. Major driving forces for the adsorption of IgG onto the PS surface come from serine (Ser), aspartic acid (Asp), and glutamic acid (Glu) residues." @default.
• W1982386830 created "2016-06-24" @default.
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• W1982386830 date "2013-07-01" @default.
• W1982386830 modified "2023-09-25" @default.
• W1982386830 title "Computational study on the interactions and orientation of monoclonal human immunoglobulin G on a polystyrene surface" @default.
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• W1982386830 doi "https://doi.org/10.2147/ijn.s44479" @default.
• W1982386830 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3713897" @default.
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• W1982386830 hasPublicationYear "2013" @default.
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