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Computational study on the interactions and orientation of monoclonal human immunoglobulin G on a polystyrene surface.

Javkhlantugs N, Bayar H, Ganzorig C, Ueda K - Int J Nanomedicine (2013)

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Center for Nanoscience and Nanotechnology and Department of Chemical Technology, School of Chemistry and Chemical Engineering, National University of Mongolia, Ulaanbaatar, Mongolia. javkhlantugs@num.edu.mn

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.

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Snapshots of the interactions between Arg residues and the PS surface included in the Fab–Fab–on orientation.Notes: Arg17 and Arg53 in b-region are shown in (A) and (B), respectively.Abbreviations: Arg, arginine; PS, polystyrene; Fab, fragment antigen-binding.
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f5-ijn-8-2487: Snapshots of the interactions between Arg residues and the PS surface included in the Fab–Fab–on orientation.Notes: Arg17 and Arg53 in b-region are shown in (A) and (B), respectively.Abbreviations: Arg, arginine; PS, polystyrene; Fab, fragment antigen-binding.

Mentions: Arg17 and Arg53 show larger interaction energy than those of Ser (Table 2). These interaction behaviors are shown in Figure 5. It can be seen that the positively charged guanidine group closely contacts with the benzene ring of the PS. This orientation indicates the existence of cation-π interaction between them. This interaction has been investigated theoretically38 and experimentally,39 using the ammonium ion and benzene derivative system. Interactions of Arg with the aromatic ring in proteins were also reported when some of the strong cation-π interactions were involved in perpendicular orientation in the protein.40 The cation-π interaction has been parameterized in the CHARMM force field.41 The parameter sets of CHARMM force field were confirmed with the quantum chemistry approaches.


Computational study on the interactions and orientation of monoclonal human immunoglobulin G on a polystyrene surface.

Javkhlantugs N, Bayar H, Ganzorig C, Ueda K - Int J Nanomedicine (2013)

Snapshots of the interactions between Arg residues and the PS surface included in the Fab–Fab–on orientation.Notes: Arg17 and Arg53 in b-region are shown in (A) and (B), respectively.Abbreviations: Arg, arginine; PS, polystyrene; Fab, fragment antigen-binding.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3713897&req=5

f5-ijn-8-2487: Snapshots of the interactions between Arg residues and the PS surface included in the Fab–Fab–on orientation.Notes: Arg17 and Arg53 in b-region are shown in (A) and (B), respectively.Abbreviations: Arg, arginine; PS, polystyrene; Fab, fragment antigen-binding.
Mentions: Arg17 and Arg53 show larger interaction energy than those of Ser (Table 2). These interaction behaviors are shown in Figure 5. It can be seen that the positively charged guanidine group closely contacts with the benzene ring of the PS. This orientation indicates the existence of cation-π interaction between them. This interaction has been investigated theoretically38 and experimentally,39 using the ammonium ion and benzene derivative system. Interactions of Arg with the aromatic ring in proteins were also reported when some of the strong cation-π interactions were involved in perpendicular orientation in the protein.40 The cation-π interaction has been parameterized in the CHARMM force field.41 The parameter sets of CHARMM force field were confirmed with the quantum chemistry approaches.

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Center for Nanoscience and Nanotechnology and Department of Chemical Technology, School of Chemistry and Chemical Engineering, National University of Mongolia, Ulaanbaatar, Mongolia. javkhlantugs@num.edu.mn

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.

Show MeSH