Negative Differential Resistance Behavior of the Iron Storage Protein Ferritin.

Realization of useful nanometer length scale devices in which metalloproteins are junction-confined in a distinct molecular arrangement for generating practical electronic signals (e.g., in bioelectronic switch configuration) is elusive till date. This is mostly due to difficulties in observing an electronically appropriate signal (i.e., reproducible and controllable), when studied under junction-assembled condition. A useful "ON"-"OFF" behavior, based on the negative differential resistance (NDR) peak characteristics in the current-voltage response curves, acquired using metal-insulator-metal (MIM) configuration, has been observed only in the case of a few proteins, namely, azurin, cytochrome c, bacteriorhodopsin, so far. The case of NDR in ferritin, an iron storage protein having a semiconducting iron core consisting of few thousands of iron atoms connected in an oxide network, has not been studied in the MIM configuration where single (or a few) molecule(s) are junction-trapped, for example, as in the case of local probe configuration of scanning probe microscopy. The present study by scanning tunneling microscopy (STM), using the naturally occurring iron-containing ferritin (human liver), as well as different iron-loaded ferritins, provides clear indication of the capability of ferritins to be NDR capable, at varying sweep conditions. As ferritin can be tailor-made in a structurally conserved manner, metal core-reconstituted ferritins, that is, Mn(III)-ferritin, Cu(II)-ferritin, and Ag-ferritin, were prepared. A correlation between the NDR peak signatures, as observed in the respective current-voltage response curves of these reconstituted ferritins, and the nature of the metal core is demonstrated. In support of our earlier proposition, here, we affirm that the ferritin protein behaves as a conductor-insulator (metal core-polypeptide shell) composite, where the overall electronic structure of the material can alter as a function of the nature of the conducting filler placed inside the insulated matrix.

Discriminating Intercalative Effects of Threading Intercalator Nogalamycin, from Classical Intercalator Daunomycin, Using Single Molecule Atomic Force Spectroscopy.

DNA threading intercalators are a unique class of intercalating agents, albeit little biophysical information is available on their intercalative actions. Herein, the intercalative effects of nogalamycin, which is a naturally-occurring DNA threading intercalator, have been investigated by high-resolution atomic force microscopy (AFM) and spectroscopy (AFS). The results have been compared with those of the well-known chemotherapeutic drug daunomycin, which is a non-threading classical intercalator bearing structural similarity to nogalamycin. A comparative AFM assessment revealed a greater increase in DNA contour length over the entire incubation period of 48 h for nogalamycin treatment, whereas the contour length increase manifested faster in case of daunomycin. The elastic response of single DNA molecules to an externally applied force was investigated by the single molecule AFS approach. Characteristic mechanical fingerprints in the overstretching behaviour clearly distinguished the nogalamycin/daunomycin-treated dsDNA from untreated dsDNA-the former appearing less elastic than the latter, and the nogalamycin-treated DNA distinguished from the daunomycin-treated DNA-the classically intercalated dsDNA appearing the least elastic. A single molecule AFS-based discrimination of threading intercalation from the classical type is being reported for the first time.

Interactions of Histone Acetyltransferase p300 with the Nuclear Proteins Histone and HMGB1, As Revealed by Single Molecule Atomic Force Spectroscopy.

One of the important properties of the transcriptional coactivator p300 is histone acetyltransferase (HAT) activity that enables p300 to influence chromatin action via histone modulation. p300 can exert its HAT action upon the other nuclear proteins too--one notable example being the transcription-factor-like protein HMGB1, which functions also as a cytokine, and whose accumulation in the cytoplasm, as a response to tissue damage, is triggered by its acetylation. Hitherto, no information on the structure and stability of the complexes between full-length p300 (p300FL) (300 kDa) and the histone/HMGB1 proteins are available, probably due to the presence of unstructured regions within p300FL that makes it difficult to be crystallized. Herein, we have adopted the high-resolution atomic force microscopy (AFM) approach, which allows molecularly resolved three-dimensional contour mapping of a protein molecule of any size and structure. From the off-rate and activation barrier values, obtained using single molecule dynamic force spectroscopy, the biochemical proposition of preferential binding of p300FL to histone H3, compared to the octameric histone, can be validated. Importantly, from the energy landscape of the dissociation events, a model for the p300-histone and the p300-HMGB1 dynamic complexes that HAT forms, can be proposed. The lower unbinding forces of the complexes observed in acetylating conditions, compared to those observed in non-acetylating conditions, indicate that upon acetylation, p300 tends to weakly associate, probably as an outcome of charge alterations on the histone/HMGB1 surface and/or acetylation-induced conformational changes. To our knowledge, for the first time, a single molecule level treatment of the interactions of HAT, where the full-length protein is considered, is being reported.

Nanostructures of Sr2+ doped BiFeO3 multifunctional ceramics with tunable photoluminescence and magnetic properties.

Careful tuning of formation (calcination) temperature of Sr(2+) doped BiFeO(3) multiferroic ceramics results in tailorable particle morphologies ranging from spherical to pillar-like. Based on the minimization of Gibb's free energy approach, the dominant homogeneous mechanism for particle growth is suggested. The chemical substitution of a trivalent ion (Bi(3+)) by a divalent ion (Sr(2+)) causes the transformation of certain fraction of Fe(3+) to Fe(4+) and/or the appearance of oxygen vacancies. This has been respectively proved by the analysis of XPS and refinement of neutron diffraction data. Although significant modification in the particle morphology is observed, the crystal unit cell remains rhombohedral with a R3c space group but interesting variations in physical properties are achieved. O-vacancies induced strong and sharp photoluminescence activity in the IR region, similar to ZnO, is reported for the first time. This observation opens up a new application for multiferroic ceramics. SQUID M-H data confirms the straightening of the canted spin structure of BiFeO(3), which in turn results in magnetism similar to ferromagnetic materials. Findings of the magneto-dielectric effect are also discussed to claim the multiferroic nature of the sample.

Optical and bio-sensing characteristics of ZnO nanotubes grown by hydrothermal method.

ZnO nanostructures were fabricated on copper substrates by hydrothermal method at an optimized growth temperature of -95 degrees C. Structural properties were investigated by field emission scanning electron and transmission electron microscopy. Distinct morphologies were found to be formed at different growth times. The formation of nanotubes mainly involved the initial nucleation followed by the growth of nanorods at 95 degrees C, and then with the increase of dissolution time at room temperature, the preferential chemical dissolution of the metastable Zn-rich [0001] polar surfaces resulted in removing the atoms from the surfaces, thus leading to the thinning of the wall of the nanostructures. Completely hollow ZnO nanotubes could be obtained at a high dissolution time. The room temperature photoluminescence and optical absorption properties of ZnO nanotubes have been studied as a function of dissolution time. The efficacy of ZnO nanotubes for glucose sensing applications has been studied.

Near-metallic behavior of warm holoferritin molecules on a gold(111) surface.

Ferritin, the iron-storage protein, holds great potential for bioelectronic applications because of the presence of an electronically conducting iron core. We have applied scanning tunneling microscopy (STM), a high-resolution imaging method based on direct tunneling, to visualize the ferritin molecules both in the iron-containing holo form and in the iron-free apo form, and we have probed the electron flow through the two forms of this protein by measuring the current-voltage response using scanning tunneling spectroscopy (STS). Clear distinctions could be made among the current-voltage responses of the metallic gold(111) substrate surface, holoferritin molecules, and apoferritin molecules at room temperature. When warmed to the near-physiological temperature of 40 °C, the current-voltage response of the holoferritin molecules exhibited no band gap resembling near-metallic behavior, and the apoferritin molecules exhibited only a reduced band gap.