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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: Having a theoretical understanding of the orientation of immunoglobulin on an immobilized solid surface is important in biomedical pathogen-detecting systems and cellular analysis.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.

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 among Glu, Asn, and Thr residues with the PS surface included in the Fc–on and Fab–Fc–on orientations.Notes: Glu309, Glu324, Glu274, Asn272, and Asn306 in c-region are shown in (A) to (E), respectively. Thr29 and Thr30 in E region are shown in (F).Abbreviations: Glu, glutamic acid; Asn, asparagine; Thr, threonine; Fab, fragment antigen-binding; Fc, fragment crystallizable.
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f7-ijn-8-2487: Snapshots of the interactions among Glu, Asn, and Thr residues with the PS surface included in the Fc–on and Fab–Fc–on orientations.Notes: Glu309, Glu324, Glu274, Asn272, and Asn306 in c-region are shown in (A) to (E), respectively. Thr29 and Thr30 in E region are shown in (F).Abbreviations: Glu, glutamic acid; Asn, asparagine; Thr, threonine; Fab, fragment antigen-binding; Fc, fragment crystallizable.

Mentions: In Fc–on orientation shown in Figure 3B, amino acid residues in HC2 domain in the Fc part of IgG1 interact with the PS surface. It was reported previously that the Fc region binds to receptors on the cell FcγR at a negatively charged area of the HC2 domain.13 In our obtained Fc–on orientation, the Asp and Glu residues in HC2 domain were found to interact strongly with a surface of PS (Table 3). The orientation behavior of these residues is shown in Figure 7A–E. The negatively charged carboxylate oxygens of residues of Glu309 and Glu324 are considered to interact with the hydrogen at the edge of the aromatic groups of PS molecules by the anionquadrupole interaction. The negatively charged residues of Asp271 and Asp303, which are shown in Table 3 but not shown in Figure 7, are also considered to have a similar interaction of anion–quadrupole interaction as was already discussed in Figure 6. On the other hand, Glu274 showed the possible orientation to have a CH/N interaction with the PS surface. The side chains of Asn272 and Asn306 are found to interact with the benzene group of the PS surface by NH/π and CH/O type interactions, respectively. There are some reports on the NH/π interaction that work between amide NH and the π electron system of the benzene group.35,43–45 All these multiple interactions, not only the anion–quadrupole interaction but also the weak NH/π and CH/O interactions, would cooperatively work as a force to bind the IgG molecule with Fc–on orientation onto the PS surface.


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 among Glu, Asn, and Thr residues with the PS surface included in the Fc–on and Fab–Fc–on orientations.Notes: Glu309, Glu324, Glu274, Asn272, and Asn306 in c-region are shown in (A) to (E), respectively. Thr29 and Thr30 in E region are shown in (F).Abbreviations: Glu, glutamic acid; Asn, asparagine; Thr, threonine; Fab, fragment antigen-binding; Fc, fragment crystallizable.
© Copyright Policy
Related In: Results  -  Collection

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

f7-ijn-8-2487: Snapshots of the interactions among Glu, Asn, and Thr residues with the PS surface included in the Fc–on and Fab–Fc–on orientations.Notes: Glu309, Glu324, Glu274, Asn272, and Asn306 in c-region are shown in (A) to (E), respectively. Thr29 and Thr30 in E region are shown in (F).Abbreviations: Glu, glutamic acid; Asn, asparagine; Thr, threonine; Fab, fragment antigen-binding; Fc, fragment crystallizable.
Mentions: In Fc–on orientation shown in Figure 3B, amino acid residues in HC2 domain in the Fc part of IgG1 interact with the PS surface. It was reported previously that the Fc region binds to receptors on the cell FcγR at a negatively charged area of the HC2 domain.13 In our obtained Fc–on orientation, the Asp and Glu residues in HC2 domain were found to interact strongly with a surface of PS (Table 3). The orientation behavior of these residues is shown in Figure 7A–E. The negatively charged carboxylate oxygens of residues of Glu309 and Glu324 are considered to interact with the hydrogen at the edge of the aromatic groups of PS molecules by the anionquadrupole interaction. The negatively charged residues of Asp271 and Asp303, which are shown in Table 3 but not shown in Figure 7, are also considered to have a similar interaction of anion–quadrupole interaction as was already discussed in Figure 6. On the other hand, Glu274 showed the possible orientation to have a CH/N interaction with the PS surface. The side chains of Asn272 and Asn306 are found to interact with the benzene group of the PS surface by NH/π and CH/O type interactions, respectively. There are some reports on the NH/π interaction that work between amide NH and the π electron system of the benzene group.35,43–45 All these multiple interactions, not only the anion–quadrupole interaction but also the weak NH/π and CH/O interactions, would cooperatively work as a force to bind the IgG molecule with Fc–on orientation onto the PS surface.

Bottom Line: Having a theoretical understanding of the orientation of immunoglobulin on an immobilized solid surface is important in biomedical pathogen-detecting systems and cellular analysis.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.

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