Interaction mechanism between soybean protein isolate and citrus pectin.

In this study, citrus pectin (CP) and soybean protein isolate (SPI) were used as raw materials to prepare a complex. The interaction mechanism and structural changes between SPI and CP were deeply studied by fluorescence spectroscopy and Fourier infrared spectroscopy. The results show that CP has a strong quenching effect on SPI's endogenous fluorescence, and with the addition of CP, the endogenous fluorescence intensity of SPI decreased from 13,565.2 to 6067.3. The CP quenching of SPI is static quenching, and the number of combined bits is 1.26. The results of three-dimensional fluorescence spectra showed that the addition of CP reduced the polarity of SPI amino acid residue microenvironment and changed the protein structure. Hydrophobic interaction exists between CP and SPI. The results of three-dimensional fluorescence spectra showed that the addition of CP reduced the polarity of the amino acid residue microenvironment of SPI and changed the protein structure. Fourier transform infrared spectroscopy shows that CP could change the secondary structure of SPI by decreasing the α-helix and ß-sheet, increasing ß-rotation and irregular curl, destroying the ordered structure of SPI and increasing the polarity of the amino acids exposed to the solution. The microstructure analysis shows that SPI-CP composite system has honeycomb structure and dense pores. From the perspective of reaction thermodynamics, it was found that the addition of CP could improve the thermal stability of SPI and increase the denaturation temperature of SPI from 119.73 to 132.97°C. This study can provide a theoretical basis for the preparation of protein-pectin complexes and provides reference for their application in food grade gels and Pickering emulsions.

Antipruritic Effect of Natural Coumarin Osthole through Selective Inhibition of Thermosensitive TRPV3 Channel in the Skin.

Coumarin osthole is a dominant bioactive ingredient of the natural Cnidium monnieri plant commonly used for traditional Chinese herbal medicines for therapies and treatments including antipruritus and antidermatitis. However, the molecular mechanism underlying the action of osthole remains unclear. In this study, we report that osthole exerts an antipruritic effect through selective inhibition of Ca2+-permeable and thermosensitive transient receptor potential vanilloid 3 (TRPV3) cation channels that are primarily expressed in the keratinocytes of the skin. Coumarin osthole was identified as an inhibitor of TRPV3 channels transiently expressed in HEK293 cells in a calcium fluorescent assay. Inhibition of the TRPV3 current by osthole and its selectivity were further confirmed by whole-cell patch clamp recordings of TRPV3-expressing HEK293 cells and mouse primary cultured keratinocytes. Behavioral evaluation demonstrated that inhibition of TRPV3 by osthole or silencing by knockout of the TRPV3 gene significantly reduced the scratching induced by either acetone-ether-water or histamine in localized rostral neck skin in mice. Taken together, our findings provide a molecular basis for use of natural coumarin osthole from the C. monnieri plant in antipruritic or skin care therapy, thus establishing a significant role of the TRPV3 channel in chronic itch signaling or acute histamine-dependent itch sensation.