Protein conformational changes revealed by optical spectroscopic reflectometry in porous silicon multilayers
Year: 2009
Authors: De Tommasi E., Rea I., Rendina I., Rotiroti L., De Stefano L.
Autors Affiliation: National Council of Research, Institute for Microelectronic and Microsystems, Department of Naples, Via P Castellino 111, I-80131 Naples, Italy
Abstract: The protein–ligand molecular interactions imply strong geometrical and structural rearrangements of the biological complex which are normally detected by high sensitivity
optical techniques such as time-resolved fluorescence microscopy. In this work, we have measured, by optical spectroscopic reflectometry in the visible–near-infrared region, the
interaction between a sugar binding protein (SBP), covalently bound on the surface of a porous silicon (PSi) microcavity, and glucose, at different concentrations and temperatures.
Variable-angle spectroscopic ellipsometric (VASE) characterization of protein-functionalized PSi layers confirms that the protein–ligand system has an overall volume smaller than the SBP alone.
Journal/Review: JOURNAL OF PHYSICS-CONDENSED MATTER
Volume: 21 (3) Pages from: 035115-1 to: 035115-5
KeyWords: Porous silicon; Biosensors; GlucoseCitations: 1data from “WEB OF SCIENCE” (of Thomson Reuters) are update at: 2024-04-28References taken from IsiWeb of Knowledge: (subscribers only)