20 research outputs found
Solid-State Protein Junctions:Cross-Laboratory Study Shows Preservation of Mechanism at Varying Electronic Coupling
Successful integration of proteins in solid-state electronics requires contacting them in a non-invasive fashion, with a solid conducting surface for immobilization as one such contact. The contacts can affect and even dominate the measured electronic transport. Often substrates, substrate treatments, protein immobilization, and device geometries differ between laboratories. Thus the question arises how far results from different laboratories and platforms are comparable and how to distinguish genuine protein electronic transport properties from platform-induced ones. We report a systematic comparison of electronic transport measurements between different laboratories, using all commonly used large-area schemes to contact a set of three proteins of largely different types. Altogether we study eight different combinations of molecular junction configurations, designed so that Ageo of junctions varies from 105 to 10−3 μm2. Although for the same protein, measured with similar device geometry, results compare reasonably well, there are significant differences in current densities (an intensive variable) between different device geometries. Likely, these originate in the critical contact-protein coupling (∼contact resistance), in addition to the actual number of proteins involved, because the effective junction contact area depends on the nanometric roughness of the electrodes and at times, even the proteins may increase this roughness. On the positive side, our results show that understanding what controls the coupling can make the coupling a design knob. In terms of extensive variables, such as temperature, our comparison unanimously shows the transport to be independent of temperature for all studied configurations and proteins. Our study places coupling and lack of temperature activation as key aspects to be considered in both modeling and practice of protein electronic transport experiments
Protein-directed reduction of graphene oxide and intracellular imaging
We demonstrate a facile, one-step, protein-directed approach to preparing a new functional reduced graphene oxide via simultaneous reduction and surface functionalization of graphene oxide sheets with herceptin and show its potential application as a novel biological imaging agent
Biomimetic crystallization of unusual macroporous calcium carbonate spherules in the presence of phosphatidylglycerol vesicles
Biomimetic Crystallization of Unusual Macroporous Calcium Carbonate Spherules in the Presence of Phosphatidylglycerol Vesicles
Revealing the role of double-layer microenvironments in pH-dependent oxygen reduction activity over metal-nitrogen-carbon catalysts
Abstract A standing puzzle in electrochemistry is that why the metal-nitrogen-carbon catalysts generally exhibit dramatic activity drop for oxygen reduction when traversing from alkaline to acid. Here, taking FeCo-N6-C double-atom catalyst as a model system and combining the ab initio molecular dynamics simulation and in situ surface-enhanced infrared absorption spectroscopy, we show that it is the significantly distinct interfacial double-layer structures, rather than the energetics of multiple reaction steps, that cause the pH-dependent oxygen reduction activity on metal-nitrogen-carbon catalysts. Specifically, the greatly disparate charge densities on electrode surfaces render different orientations of interfacial water under alkaline and acid oxygen reduction conditions, thereby affecting the formation of hydrogen bonds between the surface oxygenated intermediates and the interfacial water molecules, eventually controlling the kinetics of the proton-coupled electron transfer steps. The present findings may open new and feasible avenues for the design of advanced metal-nitrogen-carbon catalysts for proton exchange membrane fuel cells
Nanostructured thin films as surface-enhanced Raman scattering substrates
Nanoporous thin films with silver nanoparticles were synthesized with a bottom–up approach, and its potential as effective surfaceenhanced Raman scattering (SERS) substrates was demonstrated. The use of mesoporous titania films as substrates allowed to control the growth of nanoparticles on the film surface. Atomic force microscopy measurements, Ultraviolet-visible and X-ray diffraction analysis confirmed the photoreduction of Ag+ to Ag0 with the formation of nanoparticles with crystallite dimensions of 32 to 36 nm. The new substrates allowed the detection of two analytes (rhodamine B isothiocyanate and cytochrome c), present in solutions at very low concentrations, highlighting their potential in SERS sensing. Reproducibility, homogeneity, enhancement factor of the substrate, consistency of results and detection limits were also assessed
High-Resolution Single-Molecule Recognition Imaging of the Molecular Details of Ricin–Aptamer Interaction
We studied the molecular details of DNA aptamer–ricin
interactions. The toxic protein ricin molecules were immobilized on
a Au(111) surface using a <i>N</i>-hydroxysuccinimide (NHS)
ester to specifically react with lysine residues located on the ricin
B chains. A single ricin molecule was visualized in situ using the
AFM tip modified with an antiricin aptamer. Computer simulation was
used to illustrate the protein and aptamer structures, the single-molecule
ricin images on a Au(111) surface, and the binding conformations of
ricin–aptamer and ricin–antibody complexes. The various
ricin conformations on a Au(111) surface were caused by the different
lysine residues reacting with the NHS ester. It was also observed
that most of the binding sites for aptamer and antibody on the A chains
of ricin molecules were not interfered by the immobilization reaction.
The different locations of the ricin binding sites to aptamer and
antibody were also distinguished by AFM recognition images and interpreted
by simulations
Electron transport via tyrosine-doped oligo-alanine peptide junctions : role of charges and hydrogen bonding
A way of modulating the solid-state electron transport (ETp) properties of oligopeptide junctions is presented by charges and internal hydrogen bonding, which affect this process markedly. The ETp properties of a series of tyrosine (Tyr)-containing hexa-alanine peptides, self-assembled in monolayers and sandwiched between gold electrodes, are investigated in response to their protonation state. Inserting a Tyr residue into these peptides enhances the ETp carried via their junctions. Deprotonation of the Tyr-containing peptides causes a further increase of ETp efficiency that depends on this residue's position. Combined results of molecular dynamics simulations and spectroscopic experiments suggest that the increased conductance upon deprotonation is mainly a result of enhanced coupling between the charged C-terminus carboxylate group and the adjacent Au electrode. Moreover, intra-peptide hydrogen bonding of the Tyr hydroxyl to the C-terminus carboxylate reduces this coupling. Hence, the extent of such a conductance change depends on the Tyr-carboxylate distance in the peptide's sequence