A crystalline silicon surface can be made biocompatible and chemically stable by a self-assembled biofilm of proteins, the hydrophobins (HFBs) purified from the fungus Pleurotus ostreatus. The protein-modified silicon surface shows an improvement in wettability and is suitable for immobilization of other proteins. Two different proteins were successfully immobilized on the HFBs-coated chips: the bovine serum albumin and an enzyme, a laccase, which retains its catalytic activity even when bound on the chip. Variable-angle spectroscopic ellipsometry (VASE), water contact angle (WCA), and fluorescence measurements demonstrated that the proposed approach in silicon surface bioactivation is a feasible strategy for the fabrication of a new class of hybrid devices.

Bioactive modification of silicon surface using self-assembled hydrophobins from Pleurotus ostreatus

De Stefano L;Rea I;De Tommasi E;Rendina I;Giocondo M;
2009

Abstract

A crystalline silicon surface can be made biocompatible and chemically stable by a self-assembled biofilm of proteins, the hydrophobins (HFBs) purified from the fungus Pleurotus ostreatus. The protein-modified silicon surface shows an improvement in wettability and is suitable for immobilization of other proteins. Two different proteins were successfully immobilized on the HFBs-coated chips: the bovine serum albumin and an enzyme, a laccase, which retains its catalytic activity even when bound on the chip. Variable-angle spectroscopic ellipsometry (VASE), water contact angle (WCA), and fluorescence measurements demonstrated that the proposed approach in silicon surface bioactivation is a feasible strategy for the fabrication of a new class of hybrid devices.
2009
Istituto per la Microelettronica e Microsistemi - IMM
Istituto per i Processi Chimico-Fisici - IPCF
MICROARRAY SUPPORT MATERIALS
CRYSTAL-STRUCTURE
PROTEIN
LACCASE
POLY(DIMETHYLSILOXANE)
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/143341
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