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.
Protein conformational changes revealed by optical spectroscopic reflectometry in porous silicon multilayers
De Tommasi E;Rea I;Rendina I;De Stefano L
2009
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
