Fine-Tuning the Molecular Design for High-Performance Molecular Diodes Based on Pyridyl Isomers.

Better control of molecule-electrode coupling (Γ) to minimize leakage current is an effective method to optimize the functionality of molecular diodes. Herein we embedded 5 isomers of phenypyridyl derivatives, each with an N atom placed at a different position, in two electrodes to fine-tune Γ between self-assembled monolayers (SAMs) and the top electrode of EGaIn (eutectic Ga-In terminating in Ga2 O3 ). Combined with electrical tunnelling results, characterizations of electronic structures, single-level model fittings, and DFT calculations, we found that the values of Γ of SAMs formed by these isomers could be regulated by nearly 10 times, thereby contributing to the leakage current changing over about two orders of magnitude and switching the isomers from resistors to diodes with a rectification ratio (r+ =|J(+1.5 V)/J(-1.5 V)|) exceeding 200. We demonstrated that the N atom placement can be chemically engineered to tune the resistive and rectifying properties of the molecular junctions, making it possible to convert molecular resistors into rectifiers. Our study provides fundamental insights into the role of isomerism in molecular electronics and offers a new avenue for designing functional molecular devices.

Ionogel-Electrode for the Study of Protein Tunnel Junctions under Physiologically Relevant Conditions.

The study of charge transport through proteins is essential for understanding complicated electrochemical processes in biological activities while the reasons for the coexistence of tunneling and hopping phenomena in protein junctions still remain unclear. In this work, a flexible and conductive ionogel electrode is synthesized and is used as a top contact to form highly reproducible protein junctions. The junctions of proteins, including human serum albumin, cytochrome C and hemoglobin, show temperature-independent electron tunneling characteristics when the junctions are in solid states while with a different mechanism of temperature-dependent electron hopping when junctions are hydrated under physiologically relevant conditions. It is demonstrated that the solvent reorganization energy plays an important role in the electron-hopping process and experimentally shown that it requires ≈100 meV for electron hopping through one heme group inside a hydrated protein molecule connected between two electrodes.

Identification and functional characterization of thioredoxin-related protein of 14 kDa in Oncomelania hupensis, the intermediate host of Schistosoma japonicum.

Oncomelania hupensis is the unique intermediate host of the blood fluke Schistosoma japonicum, which causes schistosomiasis. In snails, highly toxic reactive oxygen species (ROS) can be continually generated by hemocytes in response to foreign particles or pathogens, and may be involved in damaging and eliminating digenean larvae. Thioredoxin-related protein of 14 kDa (TRP14) is a member of the Trx superfamily, and plays an important role in the scavenging of ROS. This study was designed to identify and characterize TRP14 from O. hupensis (OhTRP14), and investigate the involvement of OhTRP14 in the scavenging of ROS in snail host immune response to the parasite S. japonicum. Here we expressed and purified the recombinant OhTRP14 and its mutant, and rOhTRP14 displayed oxidoreductase activity dependent on the CPDC motif. OhTRP14 protein was ubiquitously present in all the tested snail tissues, and especially immunolocalized in the cytoplasm of immune cell types (hemocytes). Both the expression of OhTRP14 and ROS level increased significantly in snails following challenge with S. japonicum. The dsRNA-mediated knockdown of OhTRP14 was successfully conducted by oral feeding, and ROS production was increased by OhTRP14 knockdown, implying that OhTRP14 was involved in the scavenging of ROS in O. hupensis circulating hemocytes. Therefore, we conclude that OhTRP14 may be involved in the scavenging of ROS in snail host immune response to the parasite S. japonicum. The results expand our understanding of the interaction between this parasite and host, and lay a foundation for the establishment of Oncomelania-schistosome infection models.