Binding kinetics between soluble beta-Gal and anti-beta-Gal immobilized on chemically nanopatterned surfaces with fractal topography

Abstract

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