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

PEDRO D. CLOP; GERARDO R. MARCHESINI; PASCAL COLPO; MARIA A. PERILLO

Münster

Congreso; nanobio europe 2014; 2014

Thepresent work was aimed at providing experimental support to the correlationbetween topographic and kinetic dimensions of protein function we describedpreviously. Through electronic and colloidal nanolithographic techniques weproduced surfaces exhibiting a fractal-like pattern with a pre-determinedtopographic dimension of domains capable to bind proteins in a covalent manner(AbAntiβ-Gal).These surfaces were used as sensors to reversibly bind β-Galand enabled the kinetic study of AbAnti β-Gal -β-Gal complex formation by surface plasmonresonance (SPR) spectroscopy. Compared with the behavior of control sensors(homogeneous topography), the Ag-Ab binding kinetics in sensors produced bynanolithography showed higher capacity and broader dispersion of binding sitescharacterized by a more diffuse attractor in the kd vs. Kd phase space.