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Abstract Wound infections pose a major healthcare issue, affecting the well‐being of millions of patients worldwide. Effective intervention and on‐site detection are important in wound management. However, current approaches are hindered by time‐consuming analysis and a lack of technology for real‐time monitoring and prompt therapy delivery. In this study, a smart wound patch system (SWPS) designed for wireless closed‐loop and in‐situ wound management is presented. The SWPS integrates a microfluidic structure, an organic electrochemical transistor (OECT) based sensor, an electrical stimulation module, and a miniaturized flexible printed circuit board (FPCB). The OECT incorporates a bacteria‐responsive DNA hydrogel‐coated gate for continuous monitoring of bacterial virulence at wound sites. Real‐time detection of OECT readings and on‐demand delivery of electrical cues to accelerate wound healing is facilitated by a mobile phone application linked with an FPCB containing low‐power electronics equipped with parallel sensing and stimulation circuitry. In this proof‐of‐concept study, the functionality of the SWPS is validated and its application both in vitro and in vivo is demonstrated. This proposed system expands the arsenal of tools available for effective wound management and enables personalized treatment.

Summary: Myristoylation is a type of lipidation with important functions. Owing to the lack of high-quality antibodies against myristoylation, developing alternative methods for profiling myristoylated proteins is important. Here, we provide a protocol for metabolic labeling using click chemistry to profile myristoylated proteins in C. elegans. Our approach improves the signal/noise ratio by covalently linking the myristoylated proteins to the beads. This protocol provides a highly specific and reproducible way for enriching myristoylated proteins, which could be modified to analyze other types of lipidations.For complete details on the use and execution of this protocol, please refer to Tang et al. (2021).

Based on an experimental field study in Japan, a model was developed to simulate dissolved nitrogen in water ponded in a paddy field. As input data, the model uses meteorological data, water balance in the field, nitrogen concentration in inlet water, and the nitrogen contribution of applied fertilizer. Five model parameters need calibration. A practical application of the model is the simulation of NH 4-N and NO 2+3-N concentrations in water ponded in a paddy field. The model improves our understanding of the interactions between forms of dissolved nitrogen in ponded water and can explain the complex changes in dissolved nitrogen concentrations in water ponded on a paddy field. [ABSTRACT FROM AUTHOR]

Variations of anions (SO42-, NO3-, NO2-, Cl- and F-), cations (K+, Na+, Ca2+, Mg2+ and NH4+) and pH values in precipitation, througfall and stemflow samples collected over a four-year period (1995–1998) in Beijing (two sites Zhongguancun and Mangshan) are presented. The annual volume-weighted range of pH values were 6.57–7.11 in precipitation, 5.46–6.86 in thoughfall and 5.32–6.41 in stemflow. The fominant anion was SO$\_\{4\}^\{2-\}$, while Ca$^\{+\}$ and NH4+ were the main cations in precipitation, throughfall and stemflow. Most of ion concentrations with precipitation, throughfall and stemflow volume showed negative correlation, except for some ones. Significant correlation values were also found between ions (SO42-, NO3-, Cl-, F-, Ca2+, Mg2+ and Na+) in precipitation, throughfall and stemflow indicated the common sources of these ions such as coal combustion, automobile emission and fertilizers application. Compared to precipitation, there was an increased ion concentration in throughfall or in stemflow. Changes of ion concentrations were in Quercus liatungensis Koiz. and Pinus tabulaefornis Carr. throughfall (or stemflow) because of different crown and bark qualities of tree species. [ABSTRACT FROM AUTHOR]

Protein-protein interaction in response to environmental conditions enables sophisticated biological and biotechnological processes. Aiming toward the rational design of a pH-sensitive protein-protein interaction, we engineered pH-sensitive mutants of streptococcal protein G B1, a binder to the IgG constant region. We systematically introduced histidine residues into the binding interface to cause electrostatic repulsion on the basis of a rigid body model, Exquisite pH sensitivity of this interaction was confirmed by surface plasmon resonance and affinity chromatography employing a clinically used human IgG. The pH-sensitive mechanism of the interaction was analyzed and evaluated from kinetic, thermodynamic, and structural viewpoints. Histidine-mediated electrostatic repulsion resulted in significant loss of exothermic heat of the binding that decreased the affinity only at acidic conditions, thereby improving the pH sensitivity. The reduced binding energy was partly recovered by "enthalpy-entropy compensation." Crystal structures of the designed mutants confirmed the validity of the rigid body model on which the effective electrostatic repulsion was based. Moreover, our data suggested that the entropy gain involved exclusion of water molecules solvated in a space formed by the introduced histidine and adjacent tryptophan residue. Our findings concerning the mechanism of histidine-introduced interactions will provide a guideline for the rational design of pH-sensitive protein-protein recognition. [ABSTRACT FROM AUTHOR]