Photocatalytic technology has been considered as an efficient protocol to drive chemical reactions in a sustainable and green way. With the assistance of semiconductor-based materials, heterogeneous photocatalysis converts solar energy directly into chemical energy that can be readily stored. It has been employed in several fields including CO2 reduction, H2O splitting, and organic synthesis. Given that near-infrared (NIR) light occupies 47% of sunlight, photocatalytic systems with a NIR response are gaining more and more attention. To enhance the solar-to-chemical conversion efficiency, precise regulation of the symmetric/asymmetric nanostructures and band structures of NIR-response photocatalysts is indispensable. Under the irradiation of NIR light, the symmetric nano-morphologies (e.g., rod-like core-shell shape), asymmetric electronic structures (e.g., defect levels in band gap) and asymmetric heterojunctions (e.g., PN junctions, semiconductor-metal or semiconductor-dye composites) of designed photocatalytic systems play key roles in promoting the light absorption, the separation of electron/hole pairs, the transport of charge carriers to the surface, or the rate of surface photocatalytic reactions. This review will comprehensively analyze the four main synthesis protocols for the fabrication of NIR-response photocatalysts with improved reaction performance. The design methods involve bandgap engineering for the direct utilization of NIR photoenergy, the up-conversion of NIR light into ultraviolet/visible light, and the photothermal effect by converting NIR photons into local heat. Additionally, challenges and perspectives for the further development of heterogeneous photocatalysts with NIR response are also discussed based on their potential applications.
Myosin‐related proteins play an important role in cancer progression. However, the clinical significance, biological functions, and mechanisms of myosin 1B (MYO1B), in esophageal squamous cell carcinoma (ESCC) remain unclear. The clinical relevance of MYO1B, SNAI2, and cyclin D1 in ESCC was determined by immunohistochemistry, Oncomine, and GEPIA databases. The oncogenic roles of MYO1B were determined by CCK8, colony formation assays, wound healing, and Transwell assay. MYO1B, SNAI2, and cyclin D1 at mRNA and protein levels in ESCC cells were detected by qPCR and Western blot analysis. In our study, we found that MYO1B expression was increased in ESCC tissue samples and correlated with tumor stage, TNM stage, and poor outcomes. Functional assays indicated that depletion of MYO1B impaired oncogenesis, and enhanced chemosensitivity in ESCC. Bioinformatic analysis and mechanistic studies illustrated that SNAI2 was a key downstream effector of MYO1B. Suppression of MYO1B downregulated expression of SNAI2, thereby inhibiting the SNAI2/cyclin D1 pathway. Furthermore, a selective inhibitor of cyclin D1 activation reversed siMYO1B cells overexpressing SNAI2‐elicited aggressive phenotypes of ESCC cells. MYO1B positively correlated with SNAI2 and cyclin D1 in ESCC samples, and higher SNAI2 expression was also associated with poor prognosis in ESCC patients. Our finding demonstrated that MYO1B activates the SNAI2/cyclin D1 pathway to drive tumorigenesis and cisplatin cytotoxicity in ESCC, indicating that MYO1B is a potential therapeutic target for patients with ESCC.
The misfolding and un-natural fibrillation of proteins/peptides are associated with many conformation diseases, such as human islet amyloid polypeptide (hIAPP) in type 2 diabetes (T2D). Inspired by molecular chaperones maintaining protein homeostasis in vivo, many polymer-based artificial chaperones were introduced to regulate protein/peptide folding and fibrillation. However, the pure polymer chaperones prefer to agglomerate into large-size micelles in the physiological environment and thus lose their chaperone functions, which greatly restricts the application of polymer-based chaperones. Here, we designed and prepared a core−shell artificial chaperone based on a dozen poly-(N-isopropylacrylamide-co-N-acryloyl-O-methylated-L-arginine) (PNAMR) anchored on a gold-nanocluster (AuNC) core. The introduction of the AuNC core significantly reduced the size and enhanced the efficacy and stability of polymer-based artificial chaperones. The PNAMR@AuNCs, with a diameter of 2.5 ± 0.5 nm, demonstrated exceptional ability in maintaining the natively unfolded conformation of protein away from the misfolding and the following fibrillation by directly binding to the natively unfolded monomolecular hIAPP and hence in preventing their conversion into toxic oligomers. More excitingly, the PNAMR@AuNCs were able to restore the natural unfolded conformation of hIAPP via dissolving the β-sheet-rich hIAPP fibrils. Considering the uniform molecular mechanism of protein misfolding and fibrillation in conformation disorders, this finding provides a generic therapeutic strategy for neurodegenerative diseases and other conformation diseases by using PNAMR@AuNC artificial chaperones to restore and maintain the native conformation of amyloid proteins.
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