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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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Schematic representation (A) and minimized conformation (B) of the structure of IgG1.Notes: Two heavy (H) and two light (L) chains are shown by mauve, orange and green, blue, respectively. The H-chains are composed of one variable domain (HV) and three constant domains (HC1, HC2, HC3); L-chains are composed of one variable domain (LV) and one constant domain (LC), respectively. Minimized conformation of IgG1 is shown with face (top) and side (bottom) views in (B).Abbreviations: H, heavy chain; L, light chain; C, constant domain; V, variable; Fab, fragment antigen-binding; Fc, fragment crystallizable; S, sulfur atom.
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f1-ijn-8-2487: Schematic representation (A) and minimized conformation (B) of the structure of IgG1.Notes: Two heavy (H) and two light (L) chains are shown by mauve, orange and green, blue, respectively. The H-chains are composed of one variable domain (HV) and three constant domains (HC1, HC2, HC3); L-chains are composed of one variable domain (LV) and one constant domain (LC), respectively. Minimized conformation of IgG1 is shown with face (top) and side (bottom) views in (B).Abbreviations: H, heavy chain; L, light chain; C, constant domain; V, variable; Fab, fragment antigen-binding; Fc, fragment crystallizable; S, sulfur atom.

Mentions: The most abundant isotope of antibodies is human IgG. Among these families, immunoglobulin G1 (IgG1) is the most typical type, and it was used in our simulation. The structure of IgG1 is shown in Figure 1. It consists of two heavy (H) and two light (L) chains and is divided into three main regions. Those are one Fc and two Fab (fragment antigen-binding) domains, as shown in Figure 1A. Each Fab–domain is further categorized into variable (V) and constant (C) parts. Each H-chain is composed of one variable (HV) domain and three constant (HC1, HC2, HC3) domains. Each L-chain links to the H-chain by one interdisulfide bond. Fc–domain is a stem of the IgG, and it links to the next H-chain with three interdisulfide bonds of the hinge. As a total, the H and L chains consist of four and two intradisulfide bonds, respectively. IgG1’s structure was determined by X-ray crystallography,19 and the coordinate of the crystallographic structure is available in the Research Collaboratory for Structural Bioinformatics Protein Data Bank (PDB entry 1IGY). In this work, the amino acid residues were renumbered sequentially from 1 to 434 for each H chain and from 1 to 213 for each L chain from the original numbering of 1IGY, respectively, for clarity. In the simulation, IgG1 was constructed with protonated form at N-terminus and unprotonated form at C-terminus in all the chains, as it exists in solution with neutral pH. All histidine residues were modeled in the unionized state by being singly protonated at the N-position.


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)

Schematic representation (A) and minimized conformation (B) of the structure of IgG1.Notes: Two heavy (H) and two light (L) chains are shown by mauve, orange and green, blue, respectively. The H-chains are composed of one variable domain (HV) and three constant domains (HC1, HC2, HC3); L-chains are composed of one variable domain (LV) and one constant domain (LC), respectively. Minimized conformation of IgG1 is shown with face (top) and side (bottom) views in (B).Abbreviations: H, heavy chain; L, light chain; C, constant domain; V, variable; Fab, fragment antigen-binding; Fc, fragment crystallizable; S, sulfur atom.
© Copyright Policy
Related In: Results  -  Collection

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getmorefigures.php?uid=PMC3713897&req=5

f1-ijn-8-2487: Schematic representation (A) and minimized conformation (B) of the structure of IgG1.Notes: Two heavy (H) and two light (L) chains are shown by mauve, orange and green, blue, respectively. The H-chains are composed of one variable domain (HV) and three constant domains (HC1, HC2, HC3); L-chains are composed of one variable domain (LV) and one constant domain (LC), respectively. Minimized conformation of IgG1 is shown with face (top) and side (bottom) views in (B).Abbreviations: H, heavy chain; L, light chain; C, constant domain; V, variable; Fab, fragment antigen-binding; Fc, fragment crystallizable; S, sulfur atom.
Mentions: The most abundant isotope of antibodies is human IgG. Among these families, immunoglobulin G1 (IgG1) is the most typical type, and it was used in our simulation. The structure of IgG1 is shown in Figure 1. It consists of two heavy (H) and two light (L) chains and is divided into three main regions. Those are one Fc and two Fab (fragment antigen-binding) domains, as shown in Figure 1A. Each Fab–domain is further categorized into variable (V) and constant (C) parts. Each H-chain is composed of one variable (HV) domain and three constant (HC1, HC2, HC3) domains. Each L-chain links to the H-chain by one interdisulfide bond. Fc–domain is a stem of the IgG, and it links to the next H-chain with three interdisulfide bonds of the hinge. As a total, the H and L chains consist of four and two intradisulfide bonds, respectively. IgG1’s structure was determined by X-ray crystallography,19 and the coordinate of the crystallographic structure is available in the Research Collaboratory for Structural Bioinformatics Protein Data Bank (PDB entry 1IGY). In this work, the amino acid residues were renumbered sequentially from 1 to 434 for each H chain and from 1 to 213 for each L chain from the original numbering of 1IGY, respectively, for clarity. In the simulation, IgG1 was constructed with protonated form at N-terminus and unprotonated form at C-terminus in all the chains, as it exists in solution with neutral pH. All histidine residues were modeled in the unionized state by being singly protonated at the N-position.

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