Bioactive modification of silicon surface using self-assembled hydrophobins from Pleurotus ostreatus.
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.
De Stefano
L
L
Unit of Naples-Institute for Microelectronics and Microsystems, National Council of Research, Via P. Castellino 111, 80131 Naples, Italy. luca.destefano@na.imm.cnr.it
Rea
I
I
De Tommasi
E
E
Rendina
I
I
Rotiroti
L
L
Giocondo
M
M
Longobardi
S
S
Armenante
A
A
Giardina
P
P
D055162:Biocatalysis; D018441:Biofilms; D005656:Fungal Proteins / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D042845:Laccase / Q000378:metabolism; D020076:Pleurotus / Q000378:metabolism*; D012031:Refractometry / Q000379:methods; D012710:Serum Albumin, Bovine / Q000378:metabolism; D012825:Silicon / Q000737:chemistry*; D013500:Surface Tension; D014867:Water / Q000737:chemistry; D017155:Wettability
D005656:Fungal Proteins; D014867:Water; D012710:Serum Albumin, Bovine; D042845:Laccase; D012825:Silicon