Direct and Selective Immobilization of Proteins by Means of an Inorganic Material-Binding Peptide: Discussion on Functionalization in the Elongation to Material-Binding Peptide
ABSTRACT Using an artificial peptide library, we have identified a peptide with affinity for ZnO materials that could be used to selectively accumulate ZnO particles on polypropylene-gold plates. In this study, we fused recombinant green fluorescent protein (GFP) with this ZnO-binding peptide (ZnOBP) and then selectively immobilized the fused protein on ZnO particles. We determined an appropriate condition for selective immobilization of recombinant GFP, and the ZnO-binding function of ZnOBP-fused GFP was examined by elongating the ZnOBP tag from a single amino acid to the intact sequence. The fusion of ZnOBP with GFP enabled specific adsorption of GFP on ZnO substrates in an appropriate solution, and thermodynamic studies showed a predominantly enthalpy-dependent electrostatic interaction between ZnOBP and the ZnO surface. The ZnOBP's binding affinity for the ZnO surface increased first in terms of material selectivity and then in terms of high affinity as the GFP-fused peptide was elongated from a single amino acid to intact ZnOBP. We concluded that the enthalpy-dependent interaction between ZnOBP and ZnO was influenced by the presence of not only charged amino acids but also their surrounding residues in the ZnOBP sequence.
Conference Proceeding: Filter spectral selection for 3 wavelength optical pyrometry[show abstract] [hide abstract]
ABSTRACT: The filter spectral selection problem for a 3-wavelength optical pyrometer is analyzed in connection with the nonideal spectral distribution of infrared radiation from a high temperature body, taking into account spectral emissivity from a specific material. The level of spectral radiance is evaluated in order to maximize the ratio between the signals from three wavelengths, two at the time. A mathcad optimization procedure for filter spectral selection is proposedSemiconductor Conference, 2001. CAS 2001 Proceedings. International; 02/2001
- Angewandte Chemie International Edition 09/2011; 50(45):10585-8. · 13.73 Impact Factor
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ABSTRACT: We report that several tryptophan-rich peptides exhibit an affinity for a hydrophobic ionic liquid (IL) (1-ethyl-3-methylimidazolium bis-trifluoromethanesulfonyl imide), and that green fluorescent protein (GFP) fused to a peptides, "SSSWWSWWWW" (SW1) or "SWWWWSWWWW" (SW2), containing serine (S) and tryptophan (W) at the C terminus localized at the IL/water interface. While GFPs without W-rich peptide distributed only in water phase, SW1- and SW2-GFPs were accumulated at the interface. The localization of SW1-GFP showed biphasic behavior, and most distinctive localization was observed at 7.1 μM. The localization of SW2-GFP presumably occurred at largely lower concentration (≤0.5 μM) than that of SW1-GFP, which difference was due to the higher hydrophobicity of SW2 peptide.Journal of Bioscience and Bioengineering 02/2012; 113(2):160-5. · 1.74 Impact Factor