The plasmon coupling in a three-layered Au/SiO2/Ag nanoshell has been investigated by means of Mie scattering theory. The dipole–dipole and dipole–quadrupole Fano resonances have been observed in the extinction spectra of Au/SiO2/Ag nanoshells. With increase of the thickness of the middle layer, the dipole–dipole Fano resonance shows a blue shift and the magnitude of this Fano profile enhances while the dipole–quadrupole Fano resonance shows a red shift and reduces. With increase of the thickness of the outer shell, the dipole–dipole Fano minimum shows a blue shift and its magnitude decreases while both the energy and magnitude of dipole–quadrupole Fano resonance increase. All of the behaviors have been discussed with the plasmon hybridization model. In addition, the Au/SiO2/Ag nanoshell is found to show strong near-field enhancements in several regions, especially in the infrared region, which may provide effective applications in surface enhanced spectroscopy.

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Monoclonal antibodies (Mabs) are valuable reagents for the purification, characterization and immunolocalization of proteins. In this study, we raised Mabs against human peroxisome proliferator-activated receptors (PPARs) using baculovirus particles displaying surface glycoprotein gp64-fusion proteins as the immunizing agent. In this system, to display fusion proteins on the viral surface, the amino terminal sequences of human PPARd and PPARg2 are inserted in-frame between the signal sequence and the mature domain of the gp64 nucleotide sequence.Mabs were raised by immunization with whole virus without a purification of the target antigens. The Mabs generated by this novel method were shown to recognize not only the gp64-PPARs fusion protein, but also mature, expressed proteins by a wide variety of techniques, including immunohistochemistry, immunoblotting, and electrophoretic mobility shift assays (EMSAs). Transfection of the transfer vector containing a nucleotide sequence encoding less than 30 amino acids along with linearized baculovirus DNA allows for the production of a high affinity antibody against the corresponding mature form. This method is of potential utility in that it allows the production of valuable antibodies without the requirement of a protein purification step.