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10.1016/j.bpc.2020.106441

http://scihub22266oqcxt.onion/10.1016/j.bpc.2020.106441
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32745829!7387289!32745829
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suck abstract from ncbi

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  • Orientation of immobilized antigens on common surfaces by a simple computational model: Exposition of SARS-CoV-2 Spike protein RBD epitopes #MMPMID32745829
  • Cerofolini L; Fragai M; Luchinat C; Ravera E
  • Biophys Chem 2020[Oct]; 265 (ä): 106441 PMID32745829show ga
  • The possibility of immobilizing a protein with antigenic properties on a solid support offers significant possibilities in the development of immunosensors and vaccine formulations. For both applications, the orientation of the antigen should ensure ready accessibility of the antibodies to the epitope. However, an experimental assessment of the orientational preferences necessarily proceeds through the preparation/isolation of the antigen, the immobilization on different surfaces and one or more biophysical characterization steps. To predict a priori whether favorable orientations can be achieved or not would allow one to select the most promising experimental routes, partly mitigating the time cost towards the final product. In this manuscript, we apply a simple computational model, based on united-residue modelling, to the prediction of the orientation of the receptor binding domain of the SARS-CoV-2 spike protein on surfaces commonly used in lateral-flow devices. These calculations can account for the experimental observation that direct immobilization on gold gives sufficient exposure of the epitope to obtain a response in immunochemical assays.
  • |*Models, Molecular[MESH]
  • |Antigens/chemistry/immunology/metabolism[MESH]
  • |Betacoronavirus/*metabolism[MESH]
  • |Epitopes/*chemistry/immunology[MESH]
  • |Molecular Docking Simulation[MESH]
  • |Protein Domains[MESH]
  • |Silicon Dioxide/chemistry[MESH]
  • |Spike Glycoprotein, Coronavirus/chemistry/immunology/*metabolism[MESH]
  • |Surface Properties[MESH]


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  • suck abstract from ncbi

    106441 ä.265 2020