Binding kinetics between soluble beta-Gal and anti-beta-Gal immobilized on chemically nanopatterned surfaces with fractal topography
The present work was aimed at providing experimental support to the correlation between topographic and kinetic dimensions of protein function we described previously. Through electronic and colloidal nanolithographic techniques we produced surfaces exhibiting a fractal-like pattern with a pre-de...
Guardado en:
| Autores principales: | , , , |
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| Formato: | conferenceObject |
| Lenguaje: | Inglés |
| Publicado: |
2022
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| Materias: | |
| Acceso en línea: | http://hdl.handle.net/11086/24368 |
| Aporte de: |
| Sumario: | The present work was aimed at providing experimental support to the correlation
between topographic and kinetic dimensions of protein function we described
previously. Through electronic and colloidal nanolithographic techniques we
produced surfaces exhibiting a fractal-like pattern with a pre-determined
topographic dimension of domains capable to bind proteins in a covalent manner
(AbAntiβ -Gal).
These surfaces were used as sensors to reversibly bind β-Gal and enabled the
kinetic study of AbAnti β-Gal -β-Gal complex formation by surface plasmon resonance
(SPR) spectroscopy. Compared with the behavior of control sensors (homogeneous
topography), the Ag-Ab binding kinetics in sensors produced by nanolithography
showed higher capacity and broader dispersion of binding sites characterized by a
more diffuse attractor in the kd vs. Kd phase space |
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