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Food-dervied biopolymer nanogels have recently received considerable attention as favorable carrier systems for nutraceuticals and drugs. In the present study, new biocompatible and self-assembled acylated rapeseed protein isolate (ARPI)-based nanogels were fabricated for potential hydrophobic drug delivery by chemical acylation and heat-induced protein denaturation. The effects of the ARPI concentration, pH, heat temperature, and heat time on the physiochemical properties of self-assembled ARPI nanogels were investigated. The optimized ARPI nanogels were characterized by a hydrodiameter of 170 nm in size, spherical morphology, and light core–dark shell structure. In comparison to native rapeseed protein isolates and ARPI without the heat treatment, ARPI nanogels as a result of dual acylation and heat processes exhibited significantly altered spatial secondary and tertiary structures, increased surface hydrophobicity, and decreased free sulfhydryl contents of the protein. Such properties endow amphilic ARPI with the self-aggregating ability, resulting in the hydrophobic core with formations of covalent disulfide bonds and the hydrophilic shell with succinyl moieties exposed to the water side. Such a cross-linked structure allowed for ARPI nanogels to be resistant against a broad array of pH and ionic strength as well as lyophilization and dilution. ARPI nanogels demonstrated 95% encapsulation efficiency of hydrophobic compound curcumin and significantly increased its anticancer activity against multiple cancer cell lines.

This study described the manufacture and characterization of different levels of succinic anhydride (0-15%, w/w) on rapeseed protein isolate (RPI) films. Mechanical, barrier, optical, surface, microstructure, and thermal properties were investigated. Results showed that 5% succinylated rapeseed protein isolate (SRPI) film revealed the overall optimal properties. The mechanical and barrier properties of 5% SRPI film were enhanced significantly compared to the RPI film. The water vapor permeability values of RPI and 5% SRPI films were 0.77 and 0.32 g mm/[hour m 2 kPa], respectively. Succinylation improved the color of RPI. The contact angle of 5% SRPI film was 108.68 and was the most hydrophobic combination. Moreover, scanning electron microscopy images revealed that 5% SRPI showed a dense, homogenous, and smooth microstructure. Thermogravimetric analysis results verified a low level of succinylation strengthened the thermal resistance of SRPI films. The content of β-sheet was almost half of all secondary structures after succinylation, which was supported by analyses of Fourier transform infrared spectroscopy. Results demonstrated that succinylation could be employed to improve the properties of rapeseed protein and SRPI films have great potential to be used as edible films.

Background Aberrant lipid metabolism marks one of characteristic features of hepatocellular carcinoma (HCC). Here, we define the function and mechanism of CAND1 in lipid metabolism and progression of HCC in vitro and in vivo, and postulate CAND1/FBXO11/hnRNPA2B1 as a suitable therapeutic target for HCC. Methods We performed IHC staining, western blot analysis and prognostic analyses of CAND1 in HCC to define its prognostic value. The functions of CAND1 were evaluated through in vitro and in vivo experiments. RNA-Seq and lipidomic assays followed by serial biochemical experiments including mass spectrometry, immunoprecipitation, GST pulldown, and ubiquitination were performed to dissect the underlying mechanism. Results CAND1 was highly expressed in HCC tissues and cell lines and served as an independent prognostic risk factor for HCC. CAND1 promoted HCC cell proliferation, colony formation, migration, and invasion in vitro. CAND1 facilitated tumor growth and metastasis in vivo. Mechanism studies demonstrated that CAND1 promoted lipid synthesis through disrupting Skp1-Cul1-FBXO11 complex assembly. Furthermore, we identified hnRNPA2B1 as a novel FBXO11-binding partner mediating CAND1 function. FBXO11 directly bound to hnRNPA2B1 and promoted hnRNPA2B1 lysine 27 (K27)- and K48-linked ubiquitination and subsequent degradation. Interfering CAND1 by shRNA significantly reduced tumor burden in primary mouse liver cancer model and PDX model. Conclusions CAND1 promoted HCC and regulated lipid synthesis by upregulating hnRNPA2B1 through dissociating Skp1-Cul-FBXO11 complex, which caused hnRNPA2B1 ubiquitination and degradation. Targeting CAND1-SCFFBXO11-hnRNPA2B1 axis may be a novel strategy against HCC.