Probing the effects of surface hydrophobicity and tether orientation on antibody-antigen binding
| Autor: | Thomas A. Knotts, Derek B. Bush |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
Surface (mathematics)
Surface Properties General Physics and Astronomy Rational engineering Molecular simulation Nanotechnology Antigen-Antibody Complex 02 engineering and technology Molecular Dynamics Simulation 010402 general chemistry 01 natural sciences Structure-Activity Relationship Molecular level Physical and Theoretical Chemistry Immunoglobulin Fragments Chemistry Orientation (computer vision) Solid surface Binding process 021001 nanoscience & nanotechnology 0104 chemical sciences Biophysics Antibody antigen Muramidase 0210 nano-technology Hydrophobic and Hydrophilic Interactions Protein Binding |
| Zdroj: | The Journal of Chemical Physics. 146:155103 |
| ISSN: | 1089-7690 0021-9606 |
| DOI: | 10.1063/1.4980083 |
| Popis: | Antibody microarrays have the potential to revolutionize molecular detection for many applications, but their current use is limited by poor reliability, and efforts to change this have not yielded fruitful results. One difficulty which limits the rational engineering of next-generation devices is that little is known, at the molecular level, about the antibody-antigen binding process near solid surfaces. Atomic-level structural information is scant because typical experimental techniques (X-ray crystallography and NMR) cannot be used to image proteins bound to surfaces. To overcome this limitation, this study uses molecular simulation and an advanced, experimentally validated, coarse-grain, protein-surface model to compare fab-lysozyme binding in bulk solution and when the fab is tethered to hydrophobic and hydrophilic surfaces. The results show that the tether site in the fab, as well as the surface hydrophobicity, significantly impacts the binding process and suggests that the optimal design involves tethering fabs upright on a hydrophilic surface. The results offer an unprecedented, molecular-level picture of the binding process and give hope that the rational design of protein-microarrays is possible. |
| Databáze: | OpenAIRE |
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