The presence of heavy metal ions such as copper in the human body at certain concentrations and specific conditions can lead to the development of different diseases. The currently available analytical detection methods remain expensive, time-consuming, and often require sample pre-treatment. The development of specific and quantitative, easy-in-operation, and cost-effective devices, capable of monitoring the level of Cu²⁺ ions in environmental and physiological media, is necessary. We use silicon nanoribbon (SiNR) ion-sensitive field effect transistor (ISFET) devices modified with a Gly–Gly–His peptide for the detection of copper ions in a large concentration range. The specific binding of copper ions causes a conformational change of the ligand, and a deprotonation of secondary amine groups. By performing differential measurements, we gain a deeper insight into the details of the ion–ligand interaction. We highlight in particular the importance of considering non-specific interactions to explain the sensors’ response.

One of the main challenges to upscale the fabrication of molecular devices is to achieve a mechanically stable device with reproducible and controllable electronic features that operates at room temperature^1,2. This is crucial because structural and electronic fluctuations can lead to significant changes in the transport characteristics at the electrode–molecule interface^3,4. In this study, we report on the realization of a mechanically and electronically robust graphene-based molecular junction. Robustness was achieved by separating the requirements for mechanical and electronic stability at the molecular level. Mechanical stability was obtained by anchoring molecules directly to the substrate, rather than to graphene electrodes, using a silanization reaction. Electronic stability was achieved by adjusting the π–π orbitals overlap of the conjugated head groups between neighbouring molecules. The molecular devices exhibited stable current–voltage (I–V) characteristics up to bias voltages of 2.0 V with reproducible transport features in the temperature range from 20 to 300 K.

Peptides are very common recognition entities that are usually attached to surfaces using multistep processes. These processes require modification of the native peptides and of the substrates. Using functional groups in native peptides for their assembly on surfaces without affecting their biological activity can facilitate the preparation of biosensors. Herein, we present a simple single-step formation of native oxytocin monolayer on gold surface. These surfaces were characterized by atomic force spectroscopy, spectroscopic ellipsometry, and X-ray photoelectron spectroscopy. We took advantage of the native disulfide bridge of the oxytocin for anchoring the peptide to the Au surface, while preserving the metal-ion binding properties. Self-assembled oxytocin monolayer was used by electrochemical impedance spectroscopy for metal-ion sensing leading to subnanomolar sensitivities for zinc or copper ions.

Sulfated saccharides are an essential part of extracellular matrices, and they are involved in a large number of interactions. Sulfated saccharide matrices in organisms accumulate heavy metal ions in addition to other essential metal ions. Accumulation of heavy metal ions alters the function of the organisms and cells, resulting in severe and irreversible damage. The effect of the sulfation pattern of saccharides on heavy metal binding preferences is enigmatic because the accessibility to structurally defined sulfated saccharides is limited and because standard analytical techniques cannot be used to quantify these interactions. We developed a new strategy that combines enzymatic and chemical synthesis with surface chemistry and label‐free electrochemical sensing to study the interactions between well‐defined sulfated saccharides and heavy metal ions. By using these tools we showed that the sulfation pattern of hyaluronic acid governs their heavy metal ions binding preferences.

We report how the electron transport through a solid-state metal/Gly-Gly-His (GGH) tripeptide monolayer/metal junction and the metal/GGH work function (WF) are modified by the GGH complexation with Cu²⁺ ions. Conducting atomic force microscopy is used to measure the current–voltage histograms. The WF is characterized by combining macroscopic Kelvin probe and Kelvin probe force microscopy at the nanoscale. We observe that the complexation of Cu²⁺ ions with the GGH monolayer is highly dependent on the molecular surface density and results in opposite trends. In the case of a high-density monolayer the conformational changes are hindered by the proximity of the neighboring peptides, hence forming an insulating layer in response to copper complexation. However, the monolayers of a slightly lower density allow for the conformational change to a looped peptide wrapping the Cu-ion, which results in a more conductive monolayer. Copper-ion complexation to the high- and low-density monolayers systematically induces an increase of the WFs. Copper-ion complexation to the low-density monolayer induces an increase of electron-transport efficiency, whereas the copper-ion complexation to the high-density monolayer results in a slight decrease of electron transport. Both of the observed trends agree with first-principle calculations. Complexation of copper to the low-density GGH monolayer induces a new gap state slightly above the Au Fermi energy that is absent in the high-density monolayer.

The ability to tune the electronic properties of oxide-bearing semiconductors such as Si/SiO₂ or transparent metal oxides such as indium-tin oxide (ITO) is of great importance in both electronic and optoelectronic device applications. In this work, we describe a process that was conducted on n-type Si/SiO₂ and ITO to induce changes in the substrate work function (WF). The substrates were modified by a two-step synthesis comprising a covalent attachment of coupling agents’ monolayer followed by in situ anchoring reactions of polarizable chromophores. The coupling agents and chromophores were chosen with opposite dipole orientations, which enabled the tunability of the substrates’ WF. In the first step, two coupling agents with opposite molecular dipole were assembled. The coupling agent with a negative dipole induced a decrease in WF of modified substrates, while the coupling agent with a positive dipole produced an increase in WFs of both ITO and Si substrates. The second modification step consisted of in situ anchoring reaction of polarizable chromophores with opposite dipoles to the coupling layer. This modification led to an additional change in the WFs of both Si/SiO₂ and ITO substrates. The WF was measured by contact potential difference and modeled by density functional theory-based theoretical calculations of the WF for each of the assembly steps. A good fit was obtained between the calculated and experimental trends. This ability to design and tune the WF of ITO substrates was implemented in an organic electronic device with improved I–V characteristics in comparison to a bare ITO-based device.

Peptides are very common recognition entities that are usually attached to surfaces using multistep processes. These processes require modification of the native peptides and of the substrates. Using functional groups in native peptides for their assembly on surfaces without affecting their biological activity can facilitate the preparation of biosensors. Herein, we present a simple single-step formation of native oxytocin monolayer on gold surface. These surfaces were characterized by atomic force spectroscopy, spectroscopic ellipsometry, and X-ray photoelectron spectroscopy. We took advantage of the native disulfide bridge of the oxytocin for anchoring the peptide to the Au surface, while preserving the metal-ion binding properties. Self-assembled oxytocin monolayer was used by electrochemical impedance spectroscopy for metal-ion sensing leading to subnanomolar sensitivities for zinc or copper ions.

Sulfated saccharides are an essential part of extra-cellular matrices, and they are involved in a large number ofinteractions. Sulfated saccharide matrices in organisms accu-mulate heavy metal ions in addition to other essential metalions. Accumulation of heavy metal ions alters the functionof the organisms and cells, resulting in severe and irreversi-ble damage. The effect of the sulfation pattern of saccha-rides on heavy metal binding preferences is enigmatic be-cause the accessibility to structurally defined sulfated sac-charides is limited and because standard analytical tech-niques cannot be used to quantify these interactions. We de-veloped a new strategy that combines enzymatic andchemical synthesis with surface chemistry and label-freeelectrochemical sensing to study the interactions betweenwell-defined sulfated saccharides and heavy metal ions. Byusing these tools we showed that the sulfation pattern ofhyaluronic acid governs their heavy metal ions binding pref-erences.

We report how the electron transport through a solid-state metal/Gly-Gly-His (GGH) tripeptide monolayer/metal junction and the metal/GGH work function (WF) are modified by the GGH complexation with Cu²⁺ ions. Conducting atomic force microscopy is used to measure the current–voltage histograms. The WF is characterized by combining macroscopic Kelvin probe and Kelvin probe force microscopy at the nanoscale. We observe that the complexation of Cu²⁺ ions with the GGH monolayer is highly dependent on the molecular surface density and results in opposite trends. In the case of a high-density monolayer the conformational changes are hindered by the proximity of the neighboring peptides, hence forming an insulating layer in response to copper complexation. However, the monolayers of a slightly lower density allow for the conformational change to a looped peptide wrapping the Cu-ion, which results in a more conductive monolayer. Copper-ion complexation to the high- and low-density monolayers systematically induces an increase of the WFs. Copper-ion complexation to the low-density monolayer induces an increase of electron-transport efficiency, whereas the copper-ion complexation to the high-density monolayer results in a slight decrease of electron transport. Both of the observed trends agree with first-principle calculations. Complexation of copper to the low-density GGH monolayer induces a new gap state slightly above the Au Fermi energy that is absent in the high-density monolayer.

The ability to tune the electronic properties of oxide-bearing semiconductors such as Si/SiO₂ or transparent metal oxides such as indium-tin oxide (ITO) is of great importance in both electronic and optoelectronic device applications. In this work, we describe a process that was conducted on n-type Si/SiO₂ and ITO to induce changes in the substrate work function (WF). The substrates were modified by a two-step synthesis comprising a covalent attachment of coupling agents’ monolayer followed by in situ anchoring reactions of polarizable chromophores. The coupling agents and chromophores were chosen with opposite dipole orientations, which enabled the tunability of the substrates’ WF. In the first step, two coupling agents with opposite molecular dipole were assembled. The coupling agent with a negative dipole induced a decrease in WF of modified substrates, while the coupling agent with a positive dipole produced an increase in WFs of both ITO and Si substrates. The second modification step consisted of in situ anchoring reaction of polarizable chromophores with opposite dipoles to the coupling layer. This modification led to an additional change in the WFs of both Si/SiO₂ and ITO substrates. The WF was measured by contact potential difference and modeled by density functional theory-based theoretical calculations of the WF for each of the assembly steps. A good fit was obtained between the calculated and experimental trends. This ability to design and tune the WF of ITO substrates was implemented in an organic electronic device with improved I–V characteristics in comparison to a bare ITO-based device.