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Background and objectives: In order to investigate the effect of wheat gluten on thermal‐vacuum packaged Chinese steamed bread (CSB) quality during storage at room temperature, the wheat gluten addition levels of 0%, 1%, and 2% were set to study the effect on the protein structure, water mobility, starch retrogradation properties, and texture properties. Findings: With the addition of wheat gluten, the β‐sheet content was increased and random coil content of thermal‐vacuum packaged CSB decreased. Wheat gluten enhanced the water holding capacity of CSB and restricted water migration, resulting in a lower content of bound water and higher content of less strongly bound water and free water according to the low‐field nuclear magnetic resonance (NMR). With the increase of wheat gluten, the diffraction peak intensity and relative crystallinity reduced. The elasticity and cohesion were higher, and the hardness, gumminess, chewiness, and resilience were lower than those in the control. Conclusions: The results of this study revealed that the addition of wheat gluten can effectively inhibit moisture dispersion and starch retrogradation to delay the staling of CSB during storage. Significance and novelty: As a natural food additive, wheat gluten can not only optimize protein structure and enhance nutritional value but also extend the shelf life of CSB. Therefore, these findings will promote industrial development of CSB. [ABSTRACT FROM AUTHOR]

Thrombus formation and tissue embedding significantly impair the clinical efficacy and retrievability of temporary interventional medical devices. Herein, we report an insect sclerotization-inspired antifouling armor for tailoring temporary interventional devices with durable resistance to protein adsorption and the following protein-mediated complications. By mimicking the phenol-polyamine chemistry assisted by phenol oxidases during sclerotization, we develop a facile one-step method to crosslink bovine serum albumin (BSA) with oxidized hydrocaffeic acid (HCA), resulting in a stable and universal BSA@HCA armor. Furthermore, the surface of the BSA@HCA armor, enriched with carboxyl groups, supports the secondary grafting of polyethylene glycol (PEG), further enhancing both its antifouling performance and durability. The synergy of robustly immobilized BSA and covalently grafted PEG provide potent resistance to the adhesion of proteins, platelets, and vascular cells in vitro . In ex vivo blood circulation experiment, the armored surface reduces thrombus formation by 95 %. Moreover, the antifouling armor retained over 60 % of its fouling resistance after 28 days of immersion in PBS. Overall, our armor engineering strategy presents a promising solution for enhancing the antifouling properties and clinical performance of temporary interventional medical devices., Competing Interests: Prof. Zhilu Yang is an editorial board member for Bioactive Materials and was not involved in the editorial review or the decision to publish this article. All authors declare that there are no competing interests., (© 2023 The Authors.)

Currently, there are no clinical drugs available to treat acute kidney injury (AKI). Given the high prevalence and high mortality rate of AKI, the development of drugs to effectively treat AKI is a huge unmet medical need and a research hotspot. Although existing evidence fully demonstrates that reactive oxygen and nitrogen species (RONS) burst at the AKI site is a major contributor to AKI progression, the heterogeneity, complexity, and unique physiological structure of the kidney make most antioxidant and anti-inflammatory small molecule drugs ineffective because of the lack of kidney targeting and side effects. Recently, nanodrugs with intrinsic kidney targeting through the control of size, shape, and surface properties have opened exciting prospects for the treatment of AKI. Many antioxidant nanodrugs have emerged to address the limitations of current AKI treatments. In this review, we systematically summarized for the first time about the emerging nanodrugs that exploit the pathological and physiological features of the kidney to overcome the limitations of traditional small-molecule drugs to achieve high AKI efficacy. First, we analyzed the pathological structural characteristics of AKI and the main pathological mechanism of AKI: hypoxia, harmful substance accumulation-induced RONS burst at the renal site despite the multifactorial initiation and heterogeneity of AKI. Subsequently, we introduced the strategies used to improve renal targeting and reviewed advances of nanodrugs for AKI: nano-RONS-sacrificial agents, antioxidant nanozymes, and nanocarriers for antioxidants and anti-inflammatory drugs. These nanodrugs have demonstrated excellent therapeutic effects, such as greatly reducing oxidative stress damage, restoring renal function, and low side effects. Finally, we discussed the challenges and future directions for translating nanodrugs into clinical AKI treatment., Competing Interests: The authors declare no conflict of interest, financial or otherwise., (© 2022 The Authors.)

Although its function in mammalian gonads has been gradually recognized, the expression and function of calretinin (CALB2)-a Ca 2+ -binding protein-in the testis and ovary of fish are still unclear. Here, we identified the cDNA sequences of calb 2 in Paralichthys olivaceus ( P. olivaceus ); analyzed its gene structure and phylogenetic and syntenic relationship by bioinformatics; and investigated its tissue distribution and localization in the gonads by real-time PCR, western blotting, and immunohistochemistry. The P. olivaceus calb 2 gene has 11 exons and 10 introns, and the full-length cDNA is 1457 bp, including an open reading frame (ORF) of 816 bp encoding 271 amino acids. The CALB2 of P. olivaceus has a higher homology with Lates calcarifer (99%) compared with other species. The conserved synteny of calb 2 neighboring gene loci was also detected in fish. Real-time PCR showed that the expression of calb 2 mRNA is abundant not only in the brain, but also in the gonads, and exhibits a higher expression in the testis than in the ovary. Western blotting indicated that the CALB2 protein has a higher expression in the testis compared with the ovary. Immunohistochemistry demonstrated that the CALB2 protein appears in Leydig cells and the ovarian germ epithelium. These results reveal that calb 2 plays an important role in the gonads of P. olivaceus .