The physics of electrons, photons, and their plasmonic interactions changes greatly when one or more dimensions are reduced down to the nanometer scale 1 . For example, graphene shows unique electrical, optical, and plasmonic properties, which are tunable through gating or chemical doping 2-5 . Similarly, ultrathin metal films (UTMFs) down to atomic thickness can possess new quantum optical effects 6,7 , peculiar dielectric properties 8 , and predicted strong plasmons 9,10 . However, truly two-dimensional plasmonics in metals has so far elusive because of the difficulty in producing large areas of sufficiently thin continuous films. Thanks to a deposition technique that allows percolation even at 1 nm thickness, we demonstrate plasmons in few-nanometer gold UTMFs, with clear evidence of new dispersion regimes and large electrical tunability. Resonance peaks at 1.5-5 m wavelengths are shifted by hundreds of nanometers and amplitude-modulated by tens of per cent through gating using relatively low voltages. The results suggest ways to use metals in plasmonic applications, such as electrooptic modulation, bio-sensing, and smart windows. Main text:Since ancient times, plasmons in nanoparticles of noble metals such as silver and gold have been used to color glass, culminating during the last two decades with a remarkable broadening of the use of plasmon excitations triggered by an improved understanding of their origin and behaviour, as well as by the availability of more sophisticated means to synthesize and pattern the metals [11][12][13] . New applications promise to have an impact on the optical industry: for example, super lenses allowing unprecedented sub-diffraction-limited optical imaging 14 , metasurfaces providing on-chip functionality in ultrathin form factor 15 , light modulation 16 , compact biosensors 17 and electrochemical effects that can be used in smart windows 18 . All

Shewanella oneidensis MR-1 is purported to express outer membrane cytochromes (e.g., MtrC and OmcA) that transfer electrons directly to Fe(III) in a mineral during anaerobic respiration. A prerequisite for this type of reaction would be the formation of a stable bond between a cytochrome and an iron oxide surface. Atomic force microscopy (AFM) was used to detect whether a specific bond forms between a hematite (Fe 2 O 3 ) thin film, created with oxygen plasma-assisted molecular beam epitaxy, and recombinant MtrC or OmcA molecules coupled to gold substrates. Force spectra displayed a unique force signature indicative of a specific bond between each cytochrome and the hematite surface. The strength of the OmcA-hematite bond was approximately twice that of the MtrC-hematite bond, but direct binding to hematite was twice as favorable for MtrC. Reversible folding/unfolding reactions were observed for mechanically denatured MtrC molecules bound to hematite. The force measurements for the hematite-cytochrome pairs were compared to spectra collected for an iron oxide and S. oneidensis under anaerobic conditions. There is a strong correlation between the whole-cell and pure-protein force spectra, suggesting that the unique binding attributes of each cytochrome complement one another and allow both MtrC and OmcA to play a prominent role in the transfer of electrons to Fe(III) in minerals. Finally, by comparing the magnitudes of binding force for the whole-cell versus pure-protein data, we were able to estimate that a single bacterium of S. oneidensis (2 by 0.5 m) expresses ϳ10 4 cytochromes on its outer surface.

Antibody recognition force microscopy showed that OmcA and MtrC are expressed on the exterior surface of living Shewanella oneidensis MR-1 cells when Fe(III), including solid-phase hematite (Fe2O3), was the terminal electron acceptor. OmcA was localized to the interface between the cell and mineral. MtrC displayed a more uniform distribution across the cell surface. Both cytochromes were associated with an extracellular polymeric substance.

Medical implants, like cardiovascular devices, improve the quality of life for countless individuals but may become infected with bacteria like Staphylococcus aureus. Such infections take the form of a biofilm, a structured community of bacterial cells adherent to the surface of a solid substrate. Every biofilm begins with an attractive force or bond between bacterium and substratum. We used atomic force microscopy to probe experimentally forces between a fibronectin-coated surface (i.e., proxy for an implanted cardiac device) and fibronectin-binding receptors on the surface of individual living bacteria from each of 80 clinical isolates of S. aureus. These isolates originated from humans with infected cardiac devices (CDI; n = 26), uninfected cardiac devices (n = 20), and the anterior nares of asymptomatic subjects (n = 34). CDI isolates exhibited a distinct bindingforce signature and had specific single amino acid polymorphisms in fibronectin-binding protein A corresponding to E652D, H782Q, and K786N. In silico molecular dynamics simulations demonstrate that residues D652, Q782, and N786 in fibronectin-binding protein A form extra hydrogen bonds with fibronectin, complementing the higher binding force and energy measured by atomic force microscopy for the CDI isolates. This study is significant, because it links pathogenic bacteria biofilms from the length scale of bonds acting across a nanometer-scale space to the clinical presentation of disease at the human dimension.adhesion | binding strength | host-pathogen interaction | pacemaker | prosthesis

All microbial biofilms are initiated through direct physical contact between a bacterium and a solid surface, a step that is controlled by inter-and intramolecular forces. Atomic force microscopy and confocal laser scanning microscopy were used simultaneously to observe the formation of a bond between a fluorescent chimeric protein on the surface of a living Escherichia coli bacterium and a solid substrate in situ. The chimera was composed of a portion of outer membrane protein A (OmpA) fused to the cyan-fluorescent protein AmCyan. Sucrose gradient centrifugation and fluorescent confocal slices through bacteria demonstrated that the chimeric protein was targeted and anchored to the external cell surface. The wormlike chain theory predicted that this protein should exhibit a nonlinear force-extension "signature" consistent with the sequential unraveling of the AmCyan and OmpA domains. Experimentally measured force-extension curves revealed a unique pair of "sawtooth" features that were present when a bond formed between a silicon nitride surface (atomic force microscopy tip) and E. coli cells expressing the OmpA-AmCyan protein. The observed sawtooth pair closely matched the wormlike chain model prediction for the mechanical unfolding of the AmCyan and OmpA substructures in series. These sawteeth disappeared from the measured force-extension curves when cells were treated with proteinase K. Furthermore, these unique sawteeth were absent for a mutant stain of E. coli incapable of expressing the AmCyan protein on its outer surface. Together, these data show that specific proteins exhibit unique force signatures characteristic of the bond that is formed between a living bacterium and another surface.A nearly universal trait of bacteria is their ability to attach to solid surfaces. Attached cells often form a biofilm, which is defined as a structured community of bacteria enclosed in a self-produced polymeric matrix adherent to an inert or living surface (6). Abundant evidence suggests that proteins on the outer wall of a bacterium play a critical role in initiating contact with another surface. Surface-induced expression of genes coding for various adhesins (e.g., flagella, pili, and fimbriae) have been characterized in the literature (28,39,45,48,51,54). Many of these studies rely on the mutation of genes of interest followed by a comparative analysis of the number of cells (wild type versus mutant) that are attached to a solid substrate. While these types of studies provide detailed characterizations of the proteins involved in mediating contact with another surface, the inherent surface-sensing mechanism remains hidden. The actual mechanism that allows a bacterium to sense or perceive another surface is the physical force(s) that exists in the nanometer-scale interface between a cell and that other surface. This type of elementary force, which includes van der Waals, electrostatic, solvation, and steric interactions (21,22,26), controls the way in which a protein on a bacterium's cell wall physically touches anoth...