Phytic acid/tannic acid reinforced hydrogels with ultra-high strength for human motion monitoring and arrays.

Conductive hydrogels have been widely researched for their potential applications in soft electronic devices. Creating environmentally friendly and multifunctional high-strength hydrogels for high-performance devices remains a significant challenge. This study employs the biodegradable material polyvinyl alcohol (PVA) as the primary component, with phytic acid (PA) and tannic acid (TA) as reinforcing phases, to create a multifunctional, high-strength "green" hydrogel. Through the multiple complexations of two bio-enhancing phases with the PVA main chain, this hydrogel attains ultra-high tensile strength (9.341 MPa), substantial toughness (4.262 MJ m-3), and extensive fracture strain (> 1000%), making it a representative with both mechanical performance and antibacterial capabilities. Additionally, it exhibits a low strain sensing limit (0.5%) and excellent durability (500 cycles under 50% strain). This work introduces a novel strategy of combining biodegradable materials with biomass to fabricate multifunctional hydrogels suitable for human motion monitoring and 2D pressure distribution.

High Tensile, Antibacterial, and Conductive Hydrogel Sensor with Multiple Cross-Linked Networks Based on PVA/Sodium Alginate/Zinc Oxide.

Hydrogel sensors have attracted a lot of attention due to their great significance for biosensors and human detection, especially their antibacterial properties when in direct contact with the human body. However, it is challenging to improve mechanical and antibacterial performance simultaneously. In this study, by using ultrasonic dispersion technology to attach zinc oxide to cellulose and adding sodium alginate, a multiple cross-linking network is generated, which effectively solves this problem. The proposed poly(vinyl alcohol)/sodium alginate/zinc oxide/hydrogel sensor exhibits not only excellent biocompatibility but also high tensile properties (strain above 2000%). Besides, the sensor also has an antibacterial function (against Escherichia coli and Staphylococcus aureus). The hydrogel acts as a strain sensor and biosensor; it can also be used as a human health detection sensor; its high tensile properties can detect large tensile deformation and small changes in force, such as finger bending, knee bending, and other joint movements, and can also be used as a sound detection sensor to detect speech and breathing. This study provides a simple method to prepare hydrogel sensors that can be useful for human health detection and biosensor development.

WIP1-mediated regulation of p38 MAPK signaling attenuates pyroptosis in sepsis-associated acute kidney injury.

Wild-Type p53-Induced Phosphatase 1 (WIP1/PPM1D) is a serine/threonine phosphatase that plays a significant role in various physiological processes. However, the involvement of WIP1 in kidney remains unclear. Lipopolysaccharide (LPS) was administered to induce acute injury in mice and human kidney 2 (HK2) cells in the study. The WIP1 inhibitor, CCT007093, was administered both in vitro and in vivo to assess its effect on kidney. The single-cell sequencing (scRNA-seq) data revealed that Ppm1d mRNA reached peak on day 2 following unilateral ischemia-reperfusion injury (uni-IRI) in mice, especially in the proximal renal tubules during repair phase. Compared to the control group, WIP1 protein exhibited a significant increase in renal tubules of patients with acute tubular injury (ATI) and mice with LPS-induced acute kidney injury (AKI), as well as in LPS-injured HK2 cells. In vitro experiments showed that CCT007093 increased the protein levels of NLRP3, cleaved-Caspase1, GSDMD-N and IL-1ß in HK2 cells and further reduced the viability of LPS-stimulated HK2 cells. In vivo experiments showed that inhibition of WIP1 activity with CCT007093 further increased cleaved-Caspase1, GSDMD-N protein levels in kidney tissue from mice with LPS-induced AKI. In addition, LPS induces phosphorylation of p38 MAPK, a key regulator of pyroptosis, which is further activated by CCT007093. In conclusion, inhibition of WIP1 activity acts as a positive regulator of renal tubular pyroptosis mainly through the mediation of phospho-p38 MAPK.

New insights into the role of dipeptidyl peptidase 8 and dipeptidyl peptidase 9 and their inhibitors.

Dipeptidyl peptidase 8 (DPP8) and 9 (DPP9) are widely expressed in mammals including humans, mainly locate in the cytoplasm. The DPP8 and DPP9 (DPP8/9) belong to serine proteolytic enzymes, they can recognize and cleave N-terminal dipeptides of specific substrates if proline is at the penultimate position. Because the localization of DPP8/9 is different from that of DPP4 and the substrates for DPP8/9 are not yet completely clear, their physiological and pathological roles are still being further explored. In this article, we will review the recent research advances focusing on the expression, regulation, and functions of DPP8/9 in physiology and pathology status. Emerging research results have shown that DPP8/9 is involved in various biological processes such as cell behavior, energy metabolism, and immune regulation, which plays an essential role in maintaining normal development and physiological functions of the body. DPP8/9 is also involved in pathological processes such as tumorigenesis, inflammation, and organ fibrosis. In recent years, related research on immune cell pyroptosis has made DPP8/9 a new potential target for the treatment of hematological diseases. In addition, DPP8/9 inhibitors also have great potential in the treatment of tumors and chronic kidney disease.