RESUMEN
An emerging strategy for exploring the application of polyoxometalates (POMs) is to assemble POM clusters into open-framework materials, especially inorganic-organic hybrid three-dimensional (3D) open-framework materials, via the introduction of different organic linkers between the POM clusters. This strategy has yielded a few 3D crystalline POMs of which a typical class is the group of polyoxometalate metal-organic frameworks (POMMOFs). However, for reported POMMOFs, only coordination bonds are involved between the linkers and POM clusters, and it has not yet produced any covalently bonded polyoxometalate frameworks. Here, the concept of "covalently bonded POMs (CPOMs)" is developed. By using vanadoborates as an example, we showed that the 3D CPOMs can be obtained by a condensation reaction through the oxolation mechanism of polymer chemistry. In particular, suitable single crystals were harvested and characterized by single-crystal X-ray diffraction. This work forges a link among polymer science, POM chemistry, and open-framework materials by demonstrating that it is possible to use covalent bonds according to polymer chemistry principles to construct crystalline 3D open-framework POM materials.
RESUMEN
A new porous vanadoborate was synthesized by employing the scale chemistry theory with the vanadoborate cluster V10B28. The twofold interpenetrated lvt network was assembled with zinc-containing elliptical vanadoborate clusters and Zn polyhedra. The single lvt framework contains a three-dimensional 38×38×20 ring channel system with the pore size (24.7×12.7â Å) reaching the mesoscale, thus indicating the possibility of constructing 3D ordered mesopores with vanadoborate clusters. The porosity of the SUT-7 structure was confirmed by CO2 adsorption of the as-synthesized materials.
RESUMEN
Reactive oxygen species (ROS) are implicated in various pathological conditions due to their ability to induce oxidative damage to cellular components. In this study, we investigated the antioxidant properties of a peptide isolated from the hydrolysate of Manila clam (Ruditapes philippinarum) muscle. Purification steps yielded RPTE2-2-4, exhibiting potent scavenging activities against DPPHâ¢, HOâ¢, and O2â¢-, akin to Vitamin C. Structural analysis showed that the isolated peptide, LFKKNLLTL, exhibited characteristics associated with antioxidant activity, including a short peptide length and the presence of aromatic and hydrophobic amino acid residues. Moreover, our study demonstrated the cytoprotective effects of the peptide against H2O2-induced oxidative stress in HepG2 cells. Pretreatment with the peptide resulted in a dose-dependent reduction in intracellular ROS levels and elevation of glutathione (GSH) levels, indicating its ability to modulate cellular defense mechanisms against oxidative damage. Furthermore, the peptide stimulated the expression of the cytoprotective enzyme heme oxygenase-1 (HO-1), further reinforcing its antioxidant properties. Overall, our findings highlight the potential of the Manila clam-derived peptide as a natural antioxidant agent with therapeutic implications for oxidative stress-related diseases. Further investigation into its mechanisms of action and in vivo efficacy is warranted to validate its therapeutic potential.
RESUMEN
Betalain has been reported as water-soluble, nitrogenous pigments with biological activities. However, their sensitivity to thermal degradation limits their application during food processing. In this report, the interaction of betalain and soy protein isolate fibrils (SPI-F) was investigated through multiple microscopic and spectroscopic techniques and the thermal stability of betalain was assessed after heating treatment. AFM and TEM images showed that the complex of betalain and SPI-F was small, amorphous aggregate. Fluorescence spectroscopy revealed that SPI-F bound with betalain via hydrophobic interactions. Circular dichroism results showed the secondary structures of SPI-F was changed by betalain binding, with a decrease in α-helix (7.5-6.9%), ß-turn (13.1-12.9%) and random coil (41.1-40.7%) and an increase in ß-Sheet (38.3-39.5%). The addition of SPI-F decreased color loss and increased the thermal retention of betalain from 55.3% to 75.9%. These findings suggest that SPI-F has a protective effect on the thermal stability of betalain and facilitate the widespread application of betalain as natural colorants.