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The multivalency of basic peptides influences the level of binding to indium tin oxide (ITO) and the extent of reduction of the work function, paving the way for amelioration of the performance of optoelectronic devices by using sustainable coatings.

Bioinspired peptide assemblies are promising candidates for use as proton-conducting materials in electrochemical devices and other advanced technologies. Progress toward applications requires establishing foundational structure-function relationships for transport in these materials. This experimental-theoretical study sheds light on how the molecular structure and proton conduction are linked in three synthetic cyclic peptide nanotube assemblies that comprise the three canonical basic amino acids (lysine, arginine, and histidine). Experiments find an order of magnitude higher proton conductivity for lysine-containing peptide assemblies compared to histidine and arginine containing assemblies. The simulations indicate that, upon peptide assembly, the basic amino acid side chains are close enough to enable direct proton transfer. The proton transfer kinetics is determined in the simulations to be governed by the structure and flexibility of the side chains. Together, experiments and theory indicate that the proton mobility is the main determinant of proton conductivity, critical for the performance of peptide-based devices.

Surface layer proteins perform multiple functions in prokaryotic cells, including cellular defense, cell-shape maintenance, and regulation of import and export of materials. However, mimicking the complex and dynamic behavior of such two-dimensional biochemical systems is challenging, and hence research has so far focused mainly on the design and manipulation of the structure and functionality of protein assemblies in solution. Motivated by the new opportunities that dynamic surface layer proteins may offer for modern technology, we herein demonstrate that immobilization of coiled coil proteins onto an inorganic surface facilitates complex behavior, manifested by reversible chemical reactions that can be rapidly monitored as digital surface readouts. Using multiple chemical triggers as inputs and several surface characteristics as outputs, we can realize reversible switching and logic gate operations that are read in parallel. Moreover, using the same coiled coil protein monolayers for derivatization of nanopores drilled into silicon nitride membranes facilitates control over ion and mass transport through the pores, thereby expanding the applicability of the dynamic coiled coil system for contemporary stochastic biosensing applications.

The talk describes a bio-inspired approach to design and prepare proton conducting materials based on self-assembling short protein sequences (peptides). The effect of amino-acid side-chain and backbone conformation on proton conductivity of the peptide fibrils will be discussed. We will show that the rational design of peptides can lead to fabrication of novel type of environmentally friendly, high performance, self-assembling, proton conducting materials.

Design flexibility and modularity have emerged as powerful tools in the development of functional self-assembled peptide nanostructures. In particular, the tendency of peptides to form fibrils and nanotubes has motivated the investigation of electron and, more recently, proton transport in their fibrous films. In this study, we present a detailed characterization by impedance spectroscopy of films of self-assembled cyclic octa-d,l-α-peptide self-assembled nanotubes with amine side chains that promote proton transport. We show that the conductivity of the peptide nanotube film, which is in the range of 0.3 mS cm-1, is within the same order of magnitude as that of ultrathin films of Nafion, a benchmark proton conducting polymer. In addition, we show that while slow diffusion processes at the interface are present for both films, additional interface effects occur in the peptide nanotube films at the same rate as their bulk proton transport effects, further limiting charge transport at the interface. Overall, our studies demonstrate the great potential of using peptides as building blocks for the preparation of bioinspired supramolecular proton conducting polymers with improved conductivity with respect to that of natural systems.

Melanin pigments have various properties that are of technological interest including photo- and radiation protection, rich coloration, and electronic functions. Nevertheless, laboratory-based synthesis of melanin and melanin-like materials with morphologies and chemical structures that are specifically optimized for these applications, is currently not possible. Here, melanin-like materials that are produced by enzymatic oxidation of a supramolecular tripeptide structures that are rich in tyrosine and have a 1D morphology are demonstrated, that are retained during the oxidation process while conducting tracks form through oxidative tyrosine crosslinking. Specifically, a minimalistic self-assembling peptide, Lys-Tyr-Tyr (KYY) with strong propensity to form supramolecular fibers, is utilized. Analysis by Raman spectroscopy shows that the tyrosines are pre-organized inside these fibers and, upon enzymatic oxidation, result in connected catechols. These form 1D conducting tracks along the length of the fiber, which gives rise to a level of internal disorder, but retention of the fiber morphology. This results in highly conductive structures demonstrated to be dominated by proton conduction. This work demonstrates the ability to control oxidation but retain a well-defined fibrous morphology that does not have a known equivalent in biology, and demonstrate exceptional conductivity that is enhanced by enzymatic oxidation.

Graphene is emerging as a promising 2D material in a variety of advanced electronic and optoelectronic devices. For optimization of the performance of the devices, tuning the work function of the graphene is crucial. This work presents a modular yet straightforward way to modulate the work function of single-layer graphene using specifically designed peptides with varied amounts of amine and indole groups assembled from an aqueous solution. Molecular doping of the graphene layer and the formation of a permanent dipole at the graphene interface led to either decreasing or increasing the work function, depending on the peptide sequence. Overall, the peptide modification increases the conductivity of the graphene layer with hardly compromising its transparency. Consequently, the modification of graphene by peptides emerges as a powerful low-cost and environmentally friendly tool to control 2D materials’ electronic properties. The modularity of peptides provides a simple way to tune the electronic properties by peptide design.

Controlling charge transfer at indium-doped tin oxide (ITO)/conductive polymer junctions is of special importance for organic photovoltaic (OPV) devices and organic light emitting diodes (OLEDs), w...

Controlled modification of the semiconductor surface work function is of fundamental importance for improvements in the efficiency of (opto-)electronic devices. Binding amino acids to a semiconductor surface through their common carboxylic group offers a versatile tool for modulation of surface properties by the choice of their side chain. This approach is demonstrated here by tailoring the surface work function of indium tin oxide, one of the most abundant transparent electrodes in organic optoelectronic devices. We find that the work function can be systematically tuned by the side chain of the amino acid, resulting in either an increase or a decrease of the work function, over a large range of ∼250 meV. This side chain effect is mostly due to alteration of the dipole component perpendicular to the surface, with a generally smaller contribution for changes in surface band bending. These findings also shed light on electronic interactions at the interface between proteins and semiconductors, which are of importance for future bio-electronic devices.

Novel reinforced cross-linked lysozyme crystals containing homogeneous dispersions of single-walled carbon nanotubes (SWCNTs) have been produced and characterized. The incorporation of SWCNTs inside lysozyme crystals gives rise to reinforced hybrid materials with tunable mechanical strength and electronic conductivity, while preserving the crystal-quality and morphology. These reinforced crystals show increase catalytic activity at higher temperature, being active even above the denaturation temperature. The electron transport through the crystals have been linked to the content and distribution of SWCNTs inside the crystals. The electron conduction through the crystals is isotropic and very efficient, presenting high conductivity values up to 600 nS at very low (0.05 wt%) SWCNTs concentration. To obtain these crystals a new protocol based on the in situ crystallization of lysozyme in hybrid SWCNTs-peptide hydrogels has been developed. These peptide hydrogels have been able to homogeneously dispersed hydrophobic SWCNTs allowing first, the crystallization of the enzyme lysozyme and secondly, transferring the new properties of the inorganic component to the crystals. Taken together, these hybrid crystals represent a notorious example of the versatility of proteins as biological substrates in the generation of novel functional materials, opening the door to use them in catalysis and bioelectronics at macroscale., Projects BIO2016-74875-P and FIS2017-85954-R (Ministerio de Economía, Industria y Competitividad, MINECO, and Agencia Estatal de Investigación, AEI, Spain, co-funded by Fondo Europeo de Desarrollo Regional, FEDER, European Union) and by Junta de Andalucía (Spain) projects P12-FQM-2721 and P12-FQM-790.

Peptide fibril nanostructures have been advocated as components of future biotechnology and nanotechnology devices. However, the ability to exploit the fibril functionality for applications, such as catalysis or electron transfer, depends on the formation of well-defined architectures. Fibrils made of peptides substituted with aromatic groups are described presenting efficient electron delocalization. Peptide self-assembly under various conditions produced polymorphic fibril products presenting distinctly different conductivities. This process is driven by a collective set of hydrogen bonding, electrostatic, and π-stacking interactions, and as a result it can be directed towards formation of a distinct polymorph by using the medium to enhance specific interactions rather than the others. This method facilitates the detailed characterization of different polymorphs, and allows specific conditions to be established that lead to the polymorph with the highest conductivity.

Low cost short wavelength infrared (SWIR) photovoltaic (PV) detectors and solar cells are of very great interest, yet the main production technology today is based on costly epitaxial growth of InGaAs layers. In this study, layers of p-type, quantum confined (QC) PbS nano-domains (NDs) structure that were engineered to absorb SWIR light at 1550 nm (Eg = 0.8 eV) were fabricated from solution using the chemical bath deposition (CBD) technique. The layers were grown on top of two different n-type CdS intermediate layers (Eg = 2.4 eV) using two different CBD protocols on fluoride tin oxide (FTO) substrates. Two types of CdS/PbS heterojunction were obtained to serve as SWIR PV detectors. The two resulting devices showed similar photoluminescence behavior, but a profoundly different electrical response to SWIR illumination. One type of CdS/PbS heterojunction exhibited a PV response to SWIR light, while the other demonstrated a photo-response to SWIR light only under an applied bias. To clarify this intriguing phenomenon, and since the only difference between the two heterojunctions could be the doping level of the CdS layer, we measured the doping level of this layer by means of the surface photo voltage (SPV). This yielded different polarizations for the two devices, indicating different doping levels of the CdS for the two different fabrication protocols, which was also confirmed by Hall Effect measurements. We performed current voltage measurements under super bandgap illumination, with respect to CdS, and got an electrical response indicating a barrier free for holes transfer from the CdS to the PbS. The results indicate that the different response does, indeed, originate from variations in the band structures at the interface of the CdS/PbS heterojunction due to the different doping levels of the CdS. We found that, unlike solar cells or visible light detectors having similar structure, in SWIR photodetectors, a type I heterojunction is formed having a barrier at the interface that limits the injection of the photo-exited electrons from the QC-PbS to the CdS side. Higher n-doped CdS generates a narrow depletion region on the CdS side, with a spike like barrier that is narrow enough to enable tunneling current, leading to a PV current. Our results show that an external quantum efficiency (EQE) of ∼2% and an internal quantum efficiency (IQE) of ∼20% can be obtained, at zero bias, for CBD grown SWIR sensitive CdS/PbS-NDs heterojunctions.

Noncovalent interactions are the main driving force in the folding of proteins into a 3D functional structure. Motivated by the wish to reveal the mechanisms of the associated self-assembly processes, scientists are focusing on studying self-assembly processes of short protein segments (peptides). While this research has led to major advances in the understanding of biological and pathological process, only in recent years has the applicative potential of the resulting self-assembled peptide assemblies started to be explored. Here, major advances in the development of biomimetic supramolecular peptide assemblies as coatings, gels, and as electroactive materials, are highlighted. The guiding lines for the design of helical peptides, β strand peptides, as well as surface binding monolayer-forming peptides that can be utilized for a specific function are highlighted. Examples of their applications in diverse immerging applications in, e.g., ecology, biomedicine, and electronics, are described. Taking into account that, in addition to extraordinary design flexibility, these materials are naturally biocompatible and ecologically friendly, and their production is cost effective, the emergence of devices incorporating these biomimetic materials in the market is envisioned in the near future.

Charge transfer at the interface between the active layer and the contact is essential in any device. Transfer of electronic charges across the contact/active layer interface with metal contacts is well-understood. To this end, noble metals, such as gold or platinum, are widely used. With these contacts, ionic currents (especially protonic) are often neglected because ions and protons do not transfer across the interface between the contact and the active layer. Palladium hydride contacts have emerged as good contacts to measure proton currents because of a reversible redox reaction at the interface and subsequent absorption/desorption of H into palladium, translating the proton flow reaching the interface into an electron flow at the outer circuit. Here, we demonstrate that gold and palladium contacts also collect proton currents, especially under high relative humidity conditions because of electrochemical reactions at the interface. A marked kinetic isotope effect, which is a signature of proton currents, is observed with gold and palladium contacts, indicating both bulk and contact processes involving proton transfer. These phenomena are attributed to electrochemical processes involving water splitting at the interface. In addition to promoting charge transfer at the interface, these interfacial electrochemical processes inject charge carriers into the active layer and hence can also modulate the bulk resistivity of the materials, as was found for the studied peptide fibril films. We conclude that proton currents may not be neglected a priori when performing electronic measurements on biological and bioinspired materials with gold and palladium contacts under high humidity conditions.

The emergent technology of using nanopores for stochastic sensing of biomolecules introduces a demand for the development of simple fabrication methodologies of nanopores in solid state membranes. This process becomes particularly challenging when membranes of composite layer architecture are involved. To overcome this challenge we have employed a focused electron beam induced chemical etching process. We present here the fabrication of nanopores in silicon-on-insulator based membranes in a single step process. In this process, chemical etching of the membrane materials by XeF2 gas is locally accelerated by an electron beam, resulting in local etching, with a top membrane oxide layer preventing delocalized etching of the silicon underneath. Nanopores with a funnel or conical, 3-dimensional (3D) shape can be fabricated, depending on the duration of exposure to XeF2, and their diameter is dominated by the time of exposure to the electron beam. The demonstrated ability to form high-aspect ratio nanopores in comparably thick, multi-layered silicon based membranes allows for an easy integration into current silicon process technology and hence is attractive for implementation in biosensing lab-on-chip fabrication technologies.

The use of non-canonical amino acids is a powerful way to control protein structure. Here, we show that subtle changes to backbone composition affect the ability of a dipeptide to modify solid surface electronic properties. The extreme sensitivity of the interactions to the peptide structure suggests potential applications in improving the performance of electronic devices.

Protons and electrons are being exploited in different natural charge transfer processes. Both types of charge carriers could be, therefore, responsible for charge transport in biomimetic self-assembled peptide nanostructures. The relative contribution of each type of charge carrier is studied in the present work for fi brils self-assembled from amyloid- β derived peptide molecules, in which two non-natural thiophene-based amino acids are included. It is shown that under low humidity conditions both electrons and protons contribute to the conduction, with current ratio of 1:2 respectively, while at higher relative humidity proton transport dominates the conductance. This hybrid conduction behavior leads to a bimodal exponential dependence of the conductance on the relative humidity. Furthermore, in both cases the conductance is shown to be affected by the peptide folding state under the entire relative humidity range. This unique hybrid conductivity behavior makes self-assembled peptide nanostructures powerful building blocks for the construction of electric devices that could use either or both types of charge carriers for their function.

The incorporation of non-canonical amino acids with aromatic side chains is considered to be a promising way to improve and control the electronic properties of self-assembled peptide nanostructures. In this work, we have studied the influence of aromatic ring heteroatom on the electronic properties of amyloid β-derived peptide fiber networks. We show that the incorporation of furan instead of thiophene side chains results in only small changes in the resistivity of the peptide network, with a threefold increase in the sheet resistance and a small decrease in the contact resistance. These changes can be explained by a twofold decrease in the diameter of the self-assembled fibers. These characteristics open the way to the use of furan- instead of thiophene-based analogues as non-natural side-chain modifications of peptides for electronic applications; this makes the fibrils more biodegradable and biorenewable.

Studies of charge transport through proteins bridged between two electrodes have been the subject of intense research in recent years. However, the complex structure of proteins makes it difficult to elucidate transport mechanisms, and the use of simple peptide oligomers may be an over simplified model of the proteins. To bridge this structural gap, we present here studies of charge transport through artificial parallel coiled-coil proteins conducted in dry environment. Protein monolayers uniaxially oriented at an angle of ∼ 30° with respect to the surface normal were prepared. Current voltage measurements, obtained using conductive-probe atomic force microscopy, revealed the mechano-electronic behavior of the protein films. It was found that the low voltage conductance of the protein monolayer increases linearly with applied force, mainly due to increase in the tip contact area. Negligible compression of the films for loads below 26 nN allowed estimating a tunneling attenuation factor, β(0) , of 0.5-0.6 Å(-1) , which is akin to charge transfer by tunneling mechanism, despite the comparably large charge transport distance. These studies show that mechano-electronic behavior of proteins can shed light on their complex charge transport mechanisms, and on how these mechanisms depend on the detailed structure of the proteins. Such studies may provide insightful information on charge transfer in biological systems.

The use of proteins and peptides as part of biosensors and electronic devices has been the focus of intense research in recent years. However, despite the fact that the interface between the bioorganic molecules and the inorganic matter plays a significant role in determining the properties of such devices, information on the electronic properties of such interfaces is sparse. In this work, we demonstrate that the identity and position of single amino acid in short inorganic binding protein-segments can significantly modulate the electronic properties of semiconductor surfaces on which they are bound. Specifically, we show that the introduction of tyrosine or tryptophan, both possessing an aromatic side chain which higher occupied molecular orbitals are positioned in proximity to the edge of GaAs valence band, to the sequence of a peptide that binds to GaAs (100) results in changes of both the electron affinity and surface potential of the semiconductor. These effects were found to be more pronounced than the effects induced by the same amino acids once bound on the surface in a head-tail configuration. Furthermore, the relative magnitude of each effect was found to depend on the position of the modification in the sequence. This sequence dependent behavior is induced both indirectly by changes in the peptide surface coverage, and directly, probably, due to changes in the orientation and proximity of the tyrosine/tryptophan side group with respect to the surface due to the preferred conformation the peptide adopts on the surface. These studies reveal that despite the use of short protein oligomers and aiming at a non-natural-electronic task, the well-known relations between the proteins' structure and function is preserved. Combining the ability to tune the electronic properties at the interface with the ability to direct the growth of inorganic materials makes peptides promising building blocks for the construction of novel hybrid electronic devices and biosensors.

The advancement of diverse electrochemistry technologies depends on the development of novel proton conducting polymers. Inspired by the efficacy of proton transport through proteins, we show in this work that self-assembling peptide nanostructures may be a promising alternative for such organic proton conducting materials. We demonstrate that aromatic amino acids, which participate in charge transport in nature, unprecedentedly promote proton conduction under both high and low relative humidity conditions for D,L α-cyclic peptide nanotubes. For dehydrated networks long-range order of the assemblies, induced by the aromatic side chains, is shown to be a dominating factor for promoting conductivity. However, for hydrated networks this order of effect is less significant and conductivity can be improved by the introduction of proton donating carboxylic acid peptide side chains in addition to the aromatic side chains despite the lower order of the assemblies. Based on these observations, a novel cyclic peptide that incorporates non-natural naphthyl side chains was designed. Self-assembled nanotubes of this peptide show greatly improved dehydrated conductivity, while maintaining high conductivity under hydrated conditions. We envision that the demonstrated modularity and versatility of these bio inspired nanostructures will make them extremely attractive building blocks for the fabrication of devices for energy conversion and storage applications, as well as other applications that involve proton transport, whether dry or wet conductivity is desired.

Protein binding to surfaces is an important phenomenon in biology and in modern technological applications. Extensive experimental and theoretical research has been focused in recent years on revealing the factors that govern binding affinity to surfaces. Theoretical studies mainly focus on examining the contribution of the individual amino acids or, alternatively, the binding potential energies of the full peptide, which are unable to capture entropic contributions and neglect the dynamic nature of the system. We present here a methodology that involves the combination of nonequilibrium dynamics simulations with strategic mutation of polar residues to reveal the different factors governing the binding free energy of a peptide to a surface. Using a gold-binding peptide as an example, we show that relative binding free energies are a consequence of the balance between strong interactions of the peptide with the surface and the ability for the bulk solvent to stabilize the peptide.

It has been reported recently that kinetic energy of photoelectrons emitted from core levels decreases with decreasing of the nanocrystal size. This phenomenon is called the size shift. The size shift value is the same for donor and acceptor in the compound. The present work is aimed on the explanation of this phenomenon. Crystals of lead sulfide PbS with different size from 50 to 350 nm were grown by chemical bath deposition (CBD) technique from alkaline solution onto Si and GaAs substrates. The morphology and size of crystals were analyzed by high resolution scanning electron microscopy (HRSEM). Complex electron spectroscopy investigations of electronic structure were carried out. In recent experiments X-ray photoelectron spectroscopy (XPS) was used for determination of Pb 4f, and S 2p electronic level positions and their size shifts. To explain the observed dependences in this work, we applied the following methods: analysis of PbS valence band (VB) and Pb 5d electronic level structure in the range ∼0–30 eV by XPS, high resolution electron energy losses spectroscopy (HREELS) for analysis of band gap transformations and work function measurements by Kelvin probe microscopy for the contact potential difference (CPD). The influence of work function increasing, widening of the band gap, transformations in VB and inter-level energy distances with decreasing of nanocrystal size on the size shift function ΔE(R) is discussed.

A method to modulate the signal of field-effect transistor biosensors using an immunosorbent assay is described. A model system is used to show that binding of a secondary antibody, to which highly charged gold colloids are attached, to an analyte on the device floating gate can be used to induce strong electrostatic effects, which affect the device threshold voltage and source-drain current. This process may be used for signal amplification, with the secondary binding specificity allowing for improved signal to noise ratio, which is of great importance for early disease detection.

This study addresses the question of whether chemically deposited PbS thin films grown on GaAs(111) are affected by the oppositely terminated substrate surfaces, gallium terminated GaAs(111)A and arsenic terminated GaAs(111)B. The differences in PbS film deposition pathway in both cases of substrate surface termination were investigated using X-ray photoelectron spectroscopy (XPS), Raman scattering, and contact potential difference (CPD) measurements. The morphology, microstructure, and crystallographic orientation of the films were studied using scanning electron microscopy, X-ray diffraction, and transmission electron microscopy. XPS and CPD measurements indicated that PbS films deposited on oppositely terminated GaAs(111) surfaces possessed corresponding surface terminations, with PbS(111)B obtained on GaAs(111)B and PbS(111)A on GaAs(111)A. Subsequently, different surface oxides were detected by XPS on A and B terminated PbS(111), with lead oxide obtained on PbS(111)A and PbSO3 obtained on PbS(111)B. ...

In this review we discuss our recent efforts directed at understanding the dynamics of catalytic networks, and their utility for performing Boolean logic operations. We start by explaining the “recipe” for the design of experimental, peptide-based, replication networks, and then the approach we take for simulating their kinetics. The studied networks can be manipulated in order to facilitate molecular replication through all 2-input Boolean logic operations, and furthermore the operational catalytic pathways can be wired together to perform more complex computational modules and network motifs. Beyond just simulations and the basic experiments, we show that while in principle all the gates may be constructed, symmetry and order constraints limit the types of logic that may be practically achieved. Finally, we describe the use of adaptive networks that form logic gates by responding to changes in the environment (pH, salt, and light), and the first steps towards realization of the performance of switching and gating molecular electronic devices using the peptides.

The unique properties of peptides have led to their use in diverse applications in medicine and nanotechnology. In order to demonstrate their utility as multifunctional, selective, adhesion layers in electronic devices, we demonstrate here peptide mediated synthesis approach for the formation of continuous gold films on a silicon–oxide substrate. This is done using a dual affinity peptide (DAP), engineered to specifically bind to the substrate at one end, and nucleate the growth of gold at the other end. The resulting film is comprised of disk shaped crystalline gold nanoparticles (NPs) with a ratio of 3–4 gold atoms per peptide. Charge transfer between the NPs and the peptide results in positive charging of the NPs, with about 23% of the gold atoms, presumably located at the surface of the NPs, interacting strongly with the peptide side chains. The resistance of the film decreases during its growth, reaching a value of 14 kΩ □−1 upon the formation of a continuous film. Finally the ability to define pattern of the films on the surface is demonstrated using the peptide as an ink in a micro-contact printing process for the formation of a template pattern on which the gold film is grown. Taking into account the diversity of peptides that can be designed this work demonstrates the promises of the use of DAPs as adhesive templates in the fabrication of devices for diverse applications.

The utilization of field-effect transistor (FET) devices in biosensing applications have been extensively studied in recent years. Qualitative and quantitative understanding of the contribution of the organic layers constructed on the device gate, and the electrolyte media, on the behavior of the device is thus crucial. In this work we analyze the contribution of different organic layers on the pH sensitivity, threshold voltage, and gain of a silicon-on-insulator based FET device. We further monitor how these properties change as function of the electrolyte screening length. Our results show that in addition to electrostatic effects, changes in the amphoteric nature of the surface also affect the device threshold voltage. These effects were found to be additive for the first (3-aminopropyl)trimethoxysilane linker layer and second biotin receptor layer. For the top streptavidin protein layer, these two effects cancel each other. The number and nature of amphoteric groups on the surface, which changes upon the formation of the layers, was shown also to affect the pH sensitivity of the device. The pH sensitivity reduces with the construction of the first two layers. However, after the formation of the streptavidin protein layer, the protein's multiple charged side chains induce an increase in the sensitivity at low ionic strengths. Furthermore, the organic layers were found to influence the device gain due to their dielectric properties, reducing the gain with the successive construction of each layer. These results demonstrate the multilevel influence of organic layers on the behavior of the FET devices.

Conformational changes of proteins are widely used in nature for controlling cellular functions, including ligand binding, oligomerization, and catalysis. Despite the fact that different proteins and artificial peptides have been utilized as electron-transfer mediators in electronic devices, the unique propensity of proteins to switch between different conformations has not been used as a mechanism to control device properties and performance. Toward this aim, we have designed and prepared new dimeric coiled-coil proteins that adopt different conformations due to parallel or antiparallel relative orientations of their monomers. We show here that controlling the conformation of these proteins attached as monolayers to gold, which dictates the direction and magnitude of the molecular dipole relative to the surface, results in quantitative modulation of the gold work function. Furthermore, charge transport through the proteins as molecular bridges is controlled by the different protein conformations, producing either rectifying or ohmic-like behavior.

We describe a concise, solid support-based synthetic method for the preparation of cyclic d,l-alpha-peptides bearing 1,4,5,8-naphthalenetetracarboxylic acid diimide (NDI) side chains. Studies of the structural and photoluminescence properties of these molecules in solution show that the hydrogen bond-directed self-assembly of the cyclic d,l-alpha-peptide backbone promotes intermolecular NDI excimer formation. The efficiency of NDI charge transfer in the resulting supramolecular assemblies is shown to depend on the length of the linker between the NDI and the peptide backbone, the distal NDI substituent, and the number of NDIs incorporated in a given structure. The design rationale and synthetic strategies described here should provide a basic blueprint for a series of self-assembling cyclic d,l-alpha-peptide nanotubes with interesting optical and electronic properties.

Functional supramolecular chemistry at the single-molecule level. Single strands of DNA can be captured inside α-hemolysin transmembrane pore protein to form single-species α-HL·DNA pseudorotaxanes. This process can be used to identify a single adenine nucleotide at a specific location on a strand of DNA by the characteristic reductions in the α-HL ion conductance. This study suggests that α-HL-mediated single-molecule DNA sequencing might be fundamentally feasible.

This article presents a method for numerical computation of the degree of coverage of chemisorbates and the resultant surface band bending as a function of the ambient gas pressure, temperature, and semiconductor doping level. This method enables quantitative evaluation of the effect of chemisorption on the electronic properties of semiconductor surfaces, such as the work function and surface conductivity, which is of great importance for many applications such as solid- state chemical sensors and electro-optical devices. The method is applied for simulating the chemisorption behavior of oxygen on n-type CdS, a process that has been investigated extensively due to its impact on the photoconductive properties of CdS photodetectors. The simulation demonstrates that the chemisorption of adions saturates when the Fermi level becomes aligned with the chemisorption-induced surface states, limiting their coverage to a small fraction of a monolayer. The degree of coverage of chemisorbed adions is proportional to the square root of the doping level, while neutral adsorbates are independent of the doping level. It is shown that the chemisorption of neutral adsorbates behaves according to the well-known Langmuir model, regardless of the existence of charged species on the surface, while charged adions do not obey Langmuir’s isotherm. In addition, it is found that in depletive chemisorption processes the resultant surface band bending increases by 2.3kT (where k is the Boltzmann constant and T is the temperature) when the gas pressure increases by one order of magnitude or when the doping level increases by two orders of magnitude.

Changes in ionic current flowing through nanopores due to binding or translocation of single biopolymer molecules enable their detection and characterization. It is, however, much more challenging to detect small molecules due to their rapid and small signal signature. Here we demonstrate the use of de novo designed peptides for functionalization of nanopores that enable the detection of a small analytes at the single molecule level. The detection relies on cooperative peptide conformational change that is induced by the binding of the small molecule to a receptor domain on the peptide. This change results in alteration of the nanopore effective diameter and hence induces current perturbation signal. On the basis of this approach, we demonstrate here the detection of diethyl 4-nitrophenyl phosphate (paraoxon), a poisonous organophosphate molecule. Paraoxon binding is induced by the incorporation of the catalytic triad of acetylcholine esterase in the hydrophilic domain of a short amphiphilic peptide and promotes β-sheet assembly of the peptide both in solution and for peptide molecules immobilized on solid surfaces. Nanopores coated with this peptide allowed the detection of paraoxon at the single molecule level revealing two binding arrangements. This unique approach, hence, provides the ability to study interactions of small molecules with the corresponding engineered receptors at the single molecule level. Furthermore, the suggested versatile platform may be used for the development of highly sensitive small analytes sensors.

Pseudomorphic high electron mobility transistor structures have been characterized using surface photovoltage spectroscopy and numerical simulations. According to the effect of the electric fields in different regions of the device on the surface photovoltage spectra, a simple empirical model that correlates the spectral parameters and electrical parameters of the structure has been developed. The spectra and their analysis are shown to provide values for the electrical parameters of the structure. The sensitivity of the technique to the device electrical parameters is shown by three different examples. In these examples, the differences in doping level and surface charge have been monitored as well as the nonuniformity of doping level across the wafer.

The photovoltage (PV) response of single quantum well p-i-n structures under open circuit conditions has been studied experimentally and numerically. The numerical calculations show a monotonic increase in the PV response with decreasing well width, implying that the ensuing increase in carrier generation rate and band gap governs the PV response. The well layer has been shown to dominate the recombination of excess carriers generated throughout the structure, and their lifetime at the well has been found to be a critical structure parameter. Using a simple semi-empirical model, the effective carrier lifetimes at the well layer/interfaces for the different samples were estimated. The results demonstrate the benefits of using surface photovoltage spectroscopy for characterization and quality control of quantum well structures.

An InGaAs/GaAs/AlGaAs single quantum well graded-index-of-refraction separate-confinement hetero-structure laser has been analyzed using surface photovoltage spectroscopy (SPS) in a contactless, nondestructive way at room temperature. Numerical simulation of the resulting spectrum made it possible to extract growth parameters, such as the InGaAs well width, the well and cladding compositions, as well as important electro-optic structure data of this device, including the lasing wavelength and built-in electric field. The results highlight the power of SPS in obtaining performance parameters of actual laser devices, containing two-dimensional structures, in a contactless, nondestructive way.

An emerging new direction of research focuses on developing "self-synthesizing materials", those supramolecular structures that can promote their own formation by accelerating the synthesis of building blocks and/or an entire assembly. It was postulated recently that practical design of such systems can benefit from the ability to control the assembly of amphiphilic molecules into nanostructures. We describe here the self-assembly pathway of short amphiphilic peptides into various forms of soluble β-sheet structures--β-plates, fibrils, and hollow nanotubes--and their consequent activity as autocatalysts for the synthesis of monomeric peptides from simpler building blocks. A detailed kinetic analysis of both the self-assembly and self-replication processes allows us to suggest a full model and simulate the replication process, revealing that only specific structures, primarily fibrils that are stable within the solution for a time shorter than a few hours, can be active as catalysts. Interestingly, we have found that such a process also induces fibril reproduction, in a mechanism very similar to the propagation of prion proteins by transmission of misfolded states.

Controlling the morphology of self-assembled peptide nanostructures, particularly those based on\ud amyloid peptides, has been the focus of intense research. In order to exploit these structures in\ud electronic applications, further understanding of their electronic behavior is required. In this work, the\ud role of peptide morphology in determining electronic conduction along self-assembled peptide\ud nanofilament networks is demonstrated. The peptides used in this work were based on the sequence\ud AAKLVFF, which is an extension of a core sequence from the amyloid b peptide. We show that the\ud incorporation of a non-natural amino acid, 2-thienylalanine, instead of phenylalanine improves the\ud obtained conductance with respect to that obtained for a similar structure based on the native sequence,\ud which was not the case for the incorporation of 3-thienylalanine. Furthermore, we demonstrate that the\ud morphology of the self-assembled structures, which can be controlled by the solvent used in the\ud assembly process, strongly affects the conductance, with larger conduction obtained for a morphology\ud of long, straight filaments. Our results demonstrate that, similar to natural systems, the assembly and\ud folding of peptides could be of great importance for optimizing their function as components of\ud electronic devices. Hence, sequence design and assembly conditions can be used to control the\ud performance of peptide based structures in such electronic applications.

The self-assembly propensity of peptides has been extensively utilized in recent years for the formation of supramolecular nanostructures. In particular, the self-assembly of peptides into fibrils and nanotubes makes them promising building blocks for electronic and electro-optic applications. However, the mechanisms of charge transfer in these wire-like structures, especially in ambient conditions, are not yet fully understood. We describe here a layer-by-layer deposition methodology of short self-assembled cyclic peptide nanotubes, which results in vertically oriented nanotubes on gold substrates. Using this novel deposition methodology, we have fabricated molecular junctions with a conductive atomic force microscopy tip as a second electrode. Studies of the junctions' current-voltage characteristics as a function of the nanotube length revealed an efficient charge transfer in these supramolecular structures, with a low current attenuation constant of 0.1 A(-1), which indicate that electron transfer is dominated by hopping. Moreover, the threshold voltage to field-emission dominated transport was found to increase with peptide length in a manner that depends on the nature of the contact with the electrodes. The flexibility in the design of the peptide monomers and the ability to control their sequential order over the nanotube by means of the layer-by-layer assembly process, which is demonstrated in this work, can be used to engineer the electronic properties of self-assembled peptide nanotubes toward device applications.

Most self-replicating peptide systems are made of α-helix forming sequences. However, it has been postulated that shorter and simpler peptides may also serve as templates for replication when arranged into well-defined structures. We describe here the design and characterization of new peptides that form soluble β-sheet aggregates that serve to significantly accelerate their ligation and self-replication. We then discuss the relevance of these phenomena to early molecular evolution, in light of additional functionality associated with β-sheet assemblies.

The fabrication of nanometric pores with controlled size is important for applications such as single molecule detection. We have recently suggested the use of focused electron beam induced etching (FEBIE) for the preparation of such nanopores in silicon nitride membranes. The use of a scanning probe microscope as the electron beam source makes this technique comparably accessible, opening the way to widespread fabrication of nanopores. Since the shape of the nanopores is critically important for their performance, in this work we focus on its analysis and study the dependence of the nanopore shape on the electron beam acceleration voltage. We show that the nanopore adopts a funnel-like shape, with a central pore penetrating the entire membrane, surrounded by an extended shallow-etched region at the top of the membrane. While the internal nanopore size was found to depend on the electron acceleration voltage, the nanopore edges extended beyond the primary electron beam spot size due to long-range effects, such as radiolysis and diffusion. Moreover, the size of the peripheral-etched region was found to be less dependent on the acceleration voltage. We also found that chemical etching is the rate-limiting step of the process and is only slightly dependent on the acceleration voltage. Furthermore, due to the chemical etch process the chemical composition of the nanopore rims was found to maintain the bulk membrane composition.

Patterning of nanoparticles on solid substrates is one of the main challenges of current nanotechnology applications. The use of organic molecules as templates for the deposition of the nanoparticles makes it possible to utilize simple soft lithography techniques for patterning. Peptides appear to be powerful candidates for this job due to their versatility and design flexibility. In this work, we demonstrate the use of dual-affinity peptides, which bind both to the substrate and to the deposited nanoparticles, as single-layer linkers for the creation of multi-component nanoparticle patterns via microcontact printing processes. Controlled deposition and patterning of gold colloids or carbon nanotubes (CNTs) on silicon oxide surfaces and that of silicon oxide nanoparticles on gold surfaces have been achieved by the use of the corresponding dual-affinity peptides. Furthermore, patterning of both gold colloids and CNTs on a single substrate on predefined locations has been achieved. The suggested generic approach offers great flexibility by allowing binding of any material to a substrate of choice, provided that a peptide binding segment has been engineered for each of the inorganic components. Furthermore, the diversity of possible peptide sequences allows the formation of multi-component patterns, paving the way to fabricating complex functional structures based on peptide templates.

The fabrication of nanometric holes within thin silicon-based membranes is of great importance for various nanotechnology applications. The preparation of such holes with accurate control over their size and shape is, thus, gaining a lot of interest. In this work we demonstrate the use of a focused electron-beam-induced etching (FEBIE) process as a promising tool for the fabrication of such nanopores in silicon nitride membranes and study the process parameters. The reduction of silicon nitride by the electron beam followed by chemical etching of the residual elemental silicon results in a linear dependence of pore diameter on electron beam exposure time, enabling accurate control of nanopore size in the range of 17-200 nm in diameter. An optimal pressure of 5.3 x 10(-6) Torr for the production of smaller pores with faster process rates, as a result of mass transport effects, was found. The pore formation process is also shown to be dependent on the details of the pulsed process cycle, which control the rate of the pore extension, and its minimal and maximal size. Our results suggest that the FEBIE process may play a key role in the fabrication of nanopores for future devices both in sensing and nano-electronics applications.

Redox-promoted self-assembly of an eight-residue cyclic D,L-α-peptide bearing four 1,4,5,8-naphthalenetetracarboxylic diimide (NDI) side chains results in the formation of electronically delocalized peptide nanotubes hundreds of nm in length. The supramolecular approach described provides a rational basis for the design and fabrication of 1-D materials with potential utility in optical and electronic devices.

Incorporation of naphthalene diimide moieties as side chains of short amphiphilic peptide results in the formation of fibrils that exhibit substantial intermolecular π-stacking interactions. These interactions can be manipulated without affecting the structure. The new system is suggested as a first step towards functional self-synthesizing materials.

Porphyrins have attracted much attention as dyes for photovoltaic applications due to their remarkable light harvesting properties and tunability of electronic behaviour. The photophysical and photochemical properties of porphyrins are influenced by electron-donating or electron-withdrawing substituents that can be attached at the perimeter of the porphyrin macrocycle. The current work shows that changing the porphyrin peripheral substituents can affect the direction of interfacial charge transfer at the interface of porphyrin and Indium tin oxide (ITO), a degenerate n-type semiconductor that is commonly used as a transparent conductive electrode in organic optoelectronic devices. Soret-band excitation resulted in electron injection from the molecular layer to the ITO in all porphyrin derivatives studied, suggesting that electron injection to ITO is faster than relaxation from the porphyrin upper excited state to the lower one. However, the direction of photo-induced electron transfer in the 500–650 nm spectral range (Q-bands excitation in porphyrins) was found to depend on the peripheral substituents. This is highly relevant for photovoltaic devices, as the solar spectrum peaks in this spectral range. The charge transfer behaviour was shown to depend on the composition of the interfacial adsorbed monolayer. Therefore, it is proposed that porphyrin derivatives can be used for modulating photo-induced interfacial transport at ITO/organic layer interfaces in a predefined, controllable way.

The dependence of nanopore biosensor conductance signal on the nanopore shape makes it important to decipher the latter with high precision. We show here that the three dimensional shape of a nanopore, extracted from electron microscopy analysis, allows for modeling the conductance of the nanopore over a wide range of ionic strengths. Furthermore, we demonstrate that the dependence of the nanopore conductance on ionic strength can be used to accurately extract the nanopore shape, eliminating the need for lengthy electron microscopy analysis. The suggested methodology can be used to monitor changes in the nanopore shape and evaluate them during electrical characterization.