| Literature DB >> 19763645 |
L De Stefano1, I Rea, E De Tommasi, I Rendina, L Rotiroti, M Giocondo, S Longobardi, A Armenante, P Giardina.
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.Entities:
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Year: 2009 PMID: 19763645 DOI: 10.1140/epje/i2009-10481-y
Source DB: PubMed Journal: Eur Phys J E Soft Matter ISSN: 1292-8941 Impact factor: 1.890