The Adsorption of P2X2 Receptors Interacting with IgG Antibodies Revealed by Combined AFM Imaging and Mechanical Simulation
The adsorption of proteins onto surfaces significantly impacts biomaterials, medical devices, and biological processes. This study aims to provide insights into the irreversible adsorption process of multiprotein complexes, particularly focusing on the interaction between anti-His6 IgG antibodies an...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-12-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/25/1/336 |
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| author | Eduardo A. Santander Graciela Bravo Yuan Chang-Halabi Gabriel J. Olguín-Orellana Pamela A. Naulin Mario J. Barrera Felipe A. Montenegro Nelson P. Barrera |
| author_facet | Eduardo A. Santander Graciela Bravo Yuan Chang-Halabi Gabriel J. Olguín-Orellana Pamela A. Naulin Mario J. Barrera Felipe A. Montenegro Nelson P. Barrera |
| author_sort | Eduardo A. Santander |
| collection | DOAJ |
| description | The adsorption of proteins onto surfaces significantly impacts biomaterials, medical devices, and biological processes. This study aims to provide insights into the irreversible adsorption process of multiprotein complexes, particularly focusing on the interaction between anti-His6 IgG antibodies and the His6-tagged P2X2 receptor. Traditional approaches to understanding protein adsorption have centered around kinetic and thermodynamic models, often examining individual proteins and surface coverage, typically through Molecular Dynamics (MD) simulations. In this research, we introduce a computational approach employing Autodesk Maya 3D software for the investigation of multiprotein complexes’ adsorption behavior. Utilizing Atomic Force Microscopy (AFM) imaging and Maya 3D-based mechanical simulations, our study yields real-time structural and kinetic observations. Our combined experimental and computational findings reveal that the P2X2 receptor–IgG antibody complex likely undergoes absorption in an ‘extended’ configuration. Whereas the P2X2 receptor is less adsorbed once is complexed to the IgG antibody compared to its individual state, the opposite is observed for the antibody. This insight enhances our understanding of the role of protein–protein interactions in the process of protein adsorption. |
| first_indexed | 2024-03-08T15:05:24Z |
| format | Article |
| id | doaj.art-7f6e5c3918154caea535380bd61a6c0c |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-08T15:05:24Z |
| publishDate | 2023-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-7f6e5c3918154caea535380bd61a6c0c2024-01-10T14:59:04ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-12-0125133610.3390/ijms25010336The Adsorption of P2X2 Receptors Interacting with IgG Antibodies Revealed by Combined AFM Imaging and Mechanical SimulationEduardo A. Santander0Graciela Bravo1Yuan Chang-Halabi2Gabriel J. Olguín-Orellana3Pamela A. Naulin4Mario J. Barrera5Felipe A. Montenegro6Nelson P. Barrera7Laboratory of Nanophysiology and Structural Biology, Faculty of Biological Sciences, Pontificia Universidad Católica de Chile, Alameda 340, Santiago 8331150, ChileLaboratory of Nanophysiology and Structural Biology, Faculty of Biological Sciences, Pontificia Universidad Católica de Chile, Alameda 340, Santiago 8331150, ChileLaboratory of Nanophysiology and Structural Biology, Faculty of Biological Sciences, Pontificia Universidad Católica de Chile, Alameda 340, Santiago 8331150, ChileLaboratory of Nanophysiology and Structural Biology, Faculty of Biological Sciences, Pontificia Universidad Católica de Chile, Alameda 340, Santiago 8331150, ChileLaboratory of Nanophysiology and Structural Biology, Faculty of Biological Sciences, Pontificia Universidad Católica de Chile, Alameda 340, Santiago 8331150, ChileLaboratory of Nanophysiology and Structural Biology, Faculty of Biological Sciences, Pontificia Universidad Católica de Chile, Alameda 340, Santiago 8331150, ChileLaboratory of Nanophysiology and Structural Biology, Faculty of Biological Sciences, Pontificia Universidad Católica de Chile, Alameda 340, Santiago 8331150, ChileLaboratory of Nanophysiology and Structural Biology, Faculty of Biological Sciences, Pontificia Universidad Católica de Chile, Alameda 340, Santiago 8331150, ChileThe adsorption of proteins onto surfaces significantly impacts biomaterials, medical devices, and biological processes. This study aims to provide insights into the irreversible adsorption process of multiprotein complexes, particularly focusing on the interaction between anti-His6 IgG antibodies and the His6-tagged P2X2 receptor. Traditional approaches to understanding protein adsorption have centered around kinetic and thermodynamic models, often examining individual proteins and surface coverage, typically through Molecular Dynamics (MD) simulations. In this research, we introduce a computational approach employing Autodesk Maya 3D software for the investigation of multiprotein complexes’ adsorption behavior. Utilizing Atomic Force Microscopy (AFM) imaging and Maya 3D-based mechanical simulations, our study yields real-time structural and kinetic observations. Our combined experimental and computational findings reveal that the P2X2 receptor–IgG antibody complex likely undergoes absorption in an ‘extended’ configuration. Whereas the P2X2 receptor is less adsorbed once is complexed to the IgG antibody compared to its individual state, the opposite is observed for the antibody. This insight enhances our understanding of the role of protein–protein interactions in the process of protein adsorption.https://www.mdpi.com/1422-0067/25/1/336protein adsorptionP2X receptorprotein–protein interactionmembrane proteinAFM imagingmechanical simulation |
| spellingShingle | Eduardo A. Santander Graciela Bravo Yuan Chang-Halabi Gabriel J. Olguín-Orellana Pamela A. Naulin Mario J. Barrera Felipe A. Montenegro Nelson P. Barrera The Adsorption of P2X2 Receptors Interacting with IgG Antibodies Revealed by Combined AFM Imaging and Mechanical Simulation International Journal of Molecular Sciences protein adsorption P2X receptor protein–protein interaction membrane protein AFM imaging mechanical simulation |
| title | The Adsorption of P2X2 Receptors Interacting with IgG Antibodies Revealed by Combined AFM Imaging and Mechanical Simulation |
| title_full | The Adsorption of P2X2 Receptors Interacting with IgG Antibodies Revealed by Combined AFM Imaging and Mechanical Simulation |
| title_fullStr | The Adsorption of P2X2 Receptors Interacting with IgG Antibodies Revealed by Combined AFM Imaging and Mechanical Simulation |
| title_full_unstemmed | The Adsorption of P2X2 Receptors Interacting with IgG Antibodies Revealed by Combined AFM Imaging and Mechanical Simulation |
| title_short | The Adsorption of P2X2 Receptors Interacting with IgG Antibodies Revealed by Combined AFM Imaging and Mechanical Simulation |
| title_sort | adsorption of p2x2 receptors interacting with igg antibodies revealed by combined afm imaging and mechanical simulation |
| topic | protein adsorption P2X receptor protein–protein interaction membrane protein AFM imaging mechanical simulation |
| url | https://www.mdpi.com/1422-0067/25/1/336 |
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