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The interaction of anatase titanium dioxide (TiO(2)) nanoparticles with chemical vapour deposited graphene sheets transferred on glass substrates is investigated by using atomic force microscopy, Raman spectroscopy and imaging. Significant electronic interactions between the nanoparticles of TiO(2) and graphene were found. The changes in the graphene Raman peak positions and intensity ratios indicate that charge transfer between graphene and TiO(2) nanoparticles occurred, increasing the Raman signal of the TiO(2) nanoparticles up to five times. The normalized Raman intensity of TiO(2) nanoparticles per their volume increased with the disorder of the graphene structure. The complementary reason for the observed enhancement is that due to the higher density of states in the defect sites of graphene, a higher electron transfer occurs from the graphene to the anatase TiO(2) nanoparticles.

Epstein-Barr virus (EBV), like other DNA tumor viruses, induces an S-phase in the natural host cell, the human B lymphocyte. This is linked with blast transformation. It is believed that the EBVencoded nuclear antigen 6 (EBNA-6) is involved in the regulation of cell cycle entry. However, the possible mechanism of this regulation is not approached. In our current study, we found that EBNA-6 binds to a MRPS18-2 protein, and targets it to the nucleus. We found that MRPS18-2 binds to both hypo-and hyperphosphorylated forms of Rb protein specifically. This binding targets the small pocket of pRb, which is a site of interaction with E2F1. The MRPS18-2 competes with the binding of E2F1 to pRb, thereby raising the level of free E2F1. Our experimental data suggest that EBNA-6 may play a major role in the entry of EBV infected B cells into the S phase by binding to and raising the level of nuclear MRPS18-2, protein. This would inhibit pRb binding to E2F1 competitively and lift the block preventing S-phase entry.cell transformation ͉ cell cycle ͉ surface plasmon resonance ͉ S-phase entry

Biosensor technologies based on optical readout are widely used in protein-protein interaction studies. Here we describe a fast and simple approach to the creation of oriented interfacial architectures for surface plasmon resonance (SPR) transducers, based on conventional biochemical procedures and custom reagents. The proposed protocol permits the oriented affinity-capture of GST fusion proteins by a specific antibody which is bound to protein A, which in turn has been immobilized on the transducer surface (after the surface has been modified by guanidine thiocyanate). The applicability of the method was demonstrated by studying the interaction between retinoblastoma tumor suppressor protein (pRb) and MRS18-2 proteins. The formation of the pRb-MRS18-2 protein complex was examined and the pRb binding site (A-box-spacer-B-box) was mapped. We have also shown that MRS18-2, which was detected as the Epstein-Barr virus-encoded EBNA-6 binding partner using the yeast two-hybrid system, binds to pRb in GST pull-down assays.

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