As one kind of plant-derived extracellular vesicle, turmeric-derived exosome-like nanoparticles (TELNs) are composed of proteins, lipids, nucleic acids, and small-molecule compounds, which possess good biocompatibility and safety. They are especially rich in information from the “mother plant”, which provides more applications in biological fields. In this study, we isolated and purified TELNs using differential centrifugation and ultracentrifugation and systematically detected their physicochemical properties using multi-omics. The TELNs possessed a typical teacup-like exosome morphology, and the extraction rate was approximately 1.71 ± 0.176 mg/g. The average particle size was 183.2 ± 10.9 nm, and the average zeta potential was −17.6 ± 1.19 mV. They were rich in lipids, mainly phosphatidylethanolamine (PE) (17.4%), triglyceride (TG) (12.3%), phosphatidylinositol (PI) (9.82%), and phosphatidylcholine (PC) (7.93%). All of them are the key lipids in the exosomes. The protein content was approximately 12% (M/M), mainly curcumin synthase and other proteins involved in secondary metabolite biosynthesis. In addition, there are critical essential genes for curcumin biosynthesis, such as curcumin synthase (CURS) and diketocoenzyme A synthase (DCS). More importantly, a greater variety of small-molecule compounds, primarily curcumin and curcumin analogs such as demethoxycurcumin and volatile oleoresins such as curcuminoids, have now been revealed. In conclusion, TELNs were successfully isolated, containing 0.17% (M/M) turmeric and a large amount of chemical information, the same as the parent-of-origin plant. This is the first time combining multi-omics to analyze the characteristics and nature of the TELNs, which laid a solid material foundation for the further development of turmeric.

Collagen is the functional protein of the skin, tendons, ligaments, cartilage, bone, and connective tissue. Due to its extraordinary properties, collagen has a wide range of applications in biomedicine, tissue engineering, food, and cosmetics. In this study, we designed a functional fragment of human type I collagen (rhLCOL-I) and expressed it in Escherichia coli (E. coli) BL21(DE3) PlysS containing a thermal-induced plasmid, pBV-rhLCOL-I. The results indicated that the optimal expression level of the rhLCOL-I reached 36.3% of the total protein at 42 °C, and expressed in soluble form. In a 7 L fermentation, the yield of purified rhLCOL-I was 1.88 g/L. Interestingly, the plasmid, pBV220-rhLCOL-I, was excellently stable during the fermentation process, even in the absence of antibiotics. Functional analyses indicated that rhLCOL-I had the capacity to promote skin cell migration and adhesion in vitro and in vivo. Taken together, we developed a high-level and low-cost approach to produce collagen fragments suitable for medical applications in E. coli.

Atopic dermatitis (AD), a prevalent chronic inflammatory skin disorder, is marked by impaired skin barrier function and persistent pruritus. It significantly deteriorates patients’ quality of life, making it one of the most burdensome non-lethal skin disorders. Filaggrin plays a crucial role in the pathophysiology of barrier disruption in AD, interacting with inflammatory mediators. It is an integral part of the extracellular matrix architecture, serving to protect the skin barrier and attenuate the inflammatory cascade. In this study, we engineered a novel recombinant human filaggrin (rhFLA-10) expression vector, which was subsequently synthesized and purified. In vitro and ex vivo efficacy experiments were conducted for AD. rhFLA-10, at low concentrations (5 to 20 μg/mL), was non-toxic to HACaT cells, significantly inhibited the degranulation of P815 mast cells, and was readily absorbed by cells, thereby exerting a soothing therapeutic effect. Furthermore, rhFLA-10 demonstrated anti-inflammatory properties (p < 0.05). In vivo, efficacy experiments further substantiated that rhFLA-10 could effectively ameliorate AD in mice and facilitate the repair of damaged skin (p < 0.001). These findings underscore the considerable potential of rhFLA-10 in the treatment of AD.