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In this paper, we prove that the product of a paired calibrated set and a set of codimension 1 calibrated by a coflat calibration with small singularity set is Almgren minimal. This is motivated by the attempt to classify all possible singularities for Almgren minimal sets–Plateau's problem in the setting of sets. In particular, a direct application of the above result leads to various types of new singularities for Almgren minimal sets, e.g. the product of any paired calibrated cone (such as the cone over the d − 2 skeleton of the unit cube in R d , d ≥ 4) with homogeneous area minimizing hypercones (such as the Simons cone). [ABSTRACT FROM AUTHOR]

Thermal barrier coatings (TBCs) are widely used as insulating layers to protect the underlying metallic structure of gas turbine blades. However, the thermal cycling performance of TBCs is affected by their complex working environments, which may shorten their service life. Previous studies have shown that preparing a mesh structure in the bonding layer can relieve thermal stress and improve the bonding strength, thereby prolonging the service life of TBCs. In this paper, a micromesh structure was prepared on the surface of the bonding layer via wet etching. The microstructure and failure mechanism of the micromesh TBCs after CMAS (CaO-MgO-Al 2 O 3 -SiO 2) thermal erosion were investigated. Numerical simulation was combined with thermal shock experiments to study the stress distribution of the micromesh-structured TBCs. The results showed that the circular convex structure can effectively improve the CMAS corrosion resistance and thermal shock resistance of TBCs. [ABSTRACT FROM AUTHOR]

The application of soy protein amyloid fibrils (SAFs) to food industrialization field has received focused attention because of their advantages such as ordered supramolecular structure and anti-proteolytic properties. However, the comparatively weak gelation properties of SAFs make it difficult to form self-supporting hydrogels, limiting its potential for future applications. Additionally, the extremely acidic environment (pH 2) of SAFs hinders their practical application in the food pH range (4–7). To address this issue, a dialysis strategy was utilized to enhance the gel structure of SAFs in this paper. The SAFs were dialyzed by deionized water and zinc ions solutions with four different pHs (2, 4, 7, and 9), and the impact of various dialysates on rheological properties, water distribution, and microstructure was investigated. The results demonstrated the method significantly improved gelation properties and modified the extremely acidic environment of SAFs. Various samples were continuously deacidified during dialysis in solutions of different pHs (4, 7, and 9), transforming from pH 2 to a higher pH value. Visual images exhibited that self-supporting hydrogels can be formed by SAFs just at a low concentration of 3% (wt). SAFs-Zn2+-9 hydrogel exhibited the highest storage modulus with a 500-fold compared to SAFs-2. Notably, the SAFs-H 2 O hydrogels were fabricated without any exogenous substances, in which the storage modulus of SAFs-H 2 O-9 increased by over 300 times. AFM images demonstrated that the shift from long rigid fibrils to short flexible fibrils induced tightly entanglement among fibrils, which improved gelation performance. Moreover, the transform in pH and the incorporation of ions caused the hydrogels to show dense network structure and strong water retention capacity. The ingenious insights were provided for improving the gelation performance of SAFs and modifying the polar acidic environment in the study, fully exploiting the potential of SAFs as edible ingredients for food applications. [Display omitted] • The extremely acidic environment of SAFs was improved by dialysis strategy. • SAFs-Zn2+-9 exhibited the highest storage modulus with a 500-fold than SAFs-2. • The hydrogel dialyzed in higher pH solution showed superior gelation performance. • Zinc ions enhanced network structures and water retention capacity of hydrogels. • Zinc ions and pH synergistically modulate the morphology of SAFs. [ABSTRACT FROM AUTHOR]

Adding prefabricated seeds to the fibril formation solution can accelerate the process of fibrillation. Various variants of soy protein amyloid fibrils (SAFs) (oligomers, short fibrils, long fibrils and mature long fibrils) were employed as seeds (OL, SF, LF and MLF). These fibrils were then introduced into a solution using a homologous seeding approach. We conducted a comprehensive analysis of various aspects, including morphological characteristics, surface hydrophobicity, secondary structures, fibril conversion rate and rheological properties. The results indicated that the addition of seeds, particularly those composed of longer and more mature fibrils, played a pivotal role in accelerating the formation of rigid and extended fibrils. Mature long fibrils as seeds can shorten the formation time of long fibrils (fibril length ≥ 600 nm) from 12 to 3 h. The seeding significantly shortens the formation time of SAFs, meanwhile, this study provides insights into the intricate dynamics of amyloid fibril at homologous seeding. [Display omitted] • The acceleration of fibrillation was influenced by the presence of fibril seeds. • The mature seeds had better efficiency of promoting fibrillation. • Homologous seeding primarily followed the template assisted growth model. • The formation of rigid, long fibrils was heavily reliant on antiparallel β-sheets. [ABSTRACT FROM AUTHOR]

The incidence of allergic disease is constantly increasing, but its pathogenesis is not fully understood. Saposhnikovia divaricata (SD), called 'Fangfeng' in China, not only can be used for antipyretic, analgesic and anti-inflammatory as a traditional Chinese medicine, but also as an active ingredient in about 8% prescriptions. However, its effects on type I allergy and pseudoallergy have not been clarified. To explore the treatment and potential mechanisms of SD and its major bioactive component Prim-O-glucosylcimifugin (POG) on type I allergy and pseudoallergy in vitro and in vivo. The inhibitory effect of SD decoction and POG on type I allergy and its possible mechanism were evaluated by using RBL-2H3 cells model in vitro and the passive cutaneous anaphylaxis (PCA) mouse model in vivo. The cell degranulation of RBL-2H3 cells induced by DNP-IgE/DNP-BSA and Compound 48/80 (C48/80) was investigated, and the molecules of degranulation related signaling pathway was further detected by qRT-PCR and Western Blot analysis. Meanwhile, therapeutic effect of SD Decoction and POG were evaluated using PCA models in vivo. The molecular docking technology was conducted to explore the potential mechanisms. In cells model induced by DNP-IgE/DNP-BSA, the release rate of β-Hex in high dose of SD and POG groups were 43.79% and 57.01%, and the release amount of HA in high dose of SD and POG groups were 26.19 ng/mL and 24.20 ng/mL. They were significantly lower than that in the model group. Besides, SD decoction and POG could significantly inhibit intracellular Ca2+ increasing and cell apoptosis. But there is no obvious effect on cells degranulation induced by C48/80. The molecular docking results showed that 5-O-Methylvisamioside and POG could bind with FcεRI α with stronger binding ability, but weak binding ability to Mrgprx2. Moreover, qPCR and Western blot analyses indicated that SD could down-regulate Lyn/Syk/PLCγ, MAPK and PI3K/AKT/NF-κB signal pathway to inhibit IgE-dependent cell degranulation. In mice PCA model, both SD and POG could dose-dependently attenuate the Evans Blue extravasation, paw and ear swelling induced by DNP-IgE/DNP-BSA, but no significant inhibition under the PCA models induced by C48/80. In conclusion, SD is effective for the therapeutic of type I allergies, suggesting that SD is a potential candidate for the treatment of type I allergy, and the underlying mechanism of these effects needs to be further studied. [Display omitted] • Saposhnikovia divaricata decoction and Prim-O-glucosylcimifugin can inhibit IgE-dependent mast cells degranulation. • Saposhnikovia divaricata decoction and Prim-O-glucosylcimifugin have no effect on IgE-independent mast cells degranulation. • Saposhnikovia divaricata decoction can attenuate type I allergy in vitro and in vivo. • Saposhnikovia divaricata decoction may be a potential drug for the treatment of type I allergy. [ABSTRACT FROM AUTHOR]

We prove that, without any assumption on lower density bound or codimension, any 1-dimensional stationary varifold on any Riemannian manifold admits unique tangent behavior everywhere. [ABSTRACT FROM AUTHOR]

The fibrillation of food proteins into amyloid fibrils, which possess unique structures, is widely acknowledged as a reliable method to enhance protein functionality. Hofmeister ions are believed to play a crucial role in the structure, solubility, and stability of proteins, as well as influencing aqueous properties. Consequently, these ions profoundly impact the folding and aggregation of amyloid fibrils. Despite this, the specific influence of Hofmeister ions on the fibrillation process of soy protein amyloid fibrils (SAFs) remains unclear. This experiment employed a comprehensive approach, utilizing atomic force microscopy, Fourier transform infrared spectroscopy, Th T fluorescence, and X-ray diffraction to investigate the microstructure and morphological changes during fibrillation. Additionally, the study aimed to explore the macro functional effects through rheological analysis. The results demonstrated that kosmotropic anions (HPO 4 2− and SO 4 2−) disrupted the fibril structure, resulting in shorter and looser fibrils. However, larger protein aggregation was found to enhance the viscosity of the solution, with the loose voids contributing to the formation of hydrogel networks. On the other hand, chaotropic cations (Zn2+ and Mg2+) were observed to promote fibril winding and lengthening, resulting in a denser structure and the formation of a hydrogel. This study significantly advances our understanding of the mechanism of ion effects during fibrillation and lays the groundwork for the utilization of plant protein amyloid fibrils in the food industry. Different types of Hofmeister ions induced SAFs with different morphological structures, resulting in different hydrogel network structures. [Display omitted] • Hofmeister ions can alter the conformation and intermolecular forces of proteins. • Different Hoffmeister ions induced different modes of protein aggregation. • The final morphology of fibril was related to the way the proteins were aggregated. • The morphology and structure of fibril affected the rheological properties of solutions. [ABSTRACT FROM AUTHOR]