In this study, melanin (BgM) was obtained from Boletus griseus. The chemical composition and structure of BgM were characterized by UV-visible absorption spectrum, Fourier transform infrared spectrum, elemental analysis, nuclear magnetic resonance, pyrolysis gas chromatography mass spectrometry, and ultra-performance liquid chromatography–high resolution mass spectrometry. The percentage contents of C, H, N, S and O elements were 56.38%, 5.86%, 6.17%, 2.44%, and 28.04%, and the S/N and C/N ratios were 0.17 and 10.66, respectively. The UV-vis spectrum of BgM showed a maximum absorption peak at 214 nm. Characteristic absorption peaks were observed at 3426, 1600 and 1105 cm−1, and BgM contained phenolic hydroxyl, amidogen, carbonyl, methylene, and methyl groups. Moreover, BgM is an eumelanin, and its main skeleton has both a benzene ring and an indole, and the branched chain mainly consists of alkanes, alcohols, and fatty acids. BgM was hydrolyzed by H2O2 and four compounds were tentatively analyzed from the UPLC-MS/MS profile. The chemical structure of BgM was characterized as 5,6-dihydroxyindole eumelanin, and the condensed molecular formula is [C28(OR1)4(OR2)3H11O6N4]n.

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The friction of a solid contact typically shows a positive dependence on normal load according to classic friction laws. A few exceptions were recently observed for nanoscale single-asperity contacts. Here, we report the experimental observation of negative friction coefficient in microscale monocrystalline heterojunctions at different temperatures. The results for the interface between graphite and muscovite mica heterojunction demonstrate a robust negative friction coefficient both in loading and unloading processes. Molecular dynamics simulations reveal that the underlying mechanism is a synergetic and nontrivial redistribution of water molecules at the interface, leading to larger density and more ordered structure of the confined subnanometer-thick water film. Our results are expected to be applicable to other hydrophilic van der Waals heterojunctions.

The aim of this study was to isolate and identify the peptides with calcium‐binding capacity from the different tilapia skin gelatin enzymatic hydrolysates. The complex protease was selected and its hydrolysates were further separated using gel filtration chromatography (Sephadex G‐25) and reverse phase high‐performance liquid chromatography. Two purified peptides with strong calcium‐binding capacity were identified as Tyr‐Gly‐Thr‐Gly‐Leu (YGTGL, 509.25 Da) and Leu‐Val‐Phe‐Leu (LVFL, 490.32 Da). The calcium‐binding capacities of YGTGL and LVFL reached 76.03 and 79.50 µg/mg, respectively. The structures of the complex of purified peptides and calcium (YGTGL‐Ca and LVFL‐Ca) were characterized by ultraviolet‐visible spectroscopy (UV‐VIS), scanning electron microscopy (SEM), X‐ray diffraction (XRD), Fourier transform infrared spectroscopy (FTIR), and mass spectrometry (LC‐MS/MS). The results of UV‐VIS, SEM, and XRD indicated that YGTGL‐Ca and LVFL‐Ca were formed as new compounds. The results of FTIR and LC‐MS/MS indicated the nitrogen atom of the amino group and the oxygen atom of the carboxyl group in terminates of the peptides provided primary binding sites. Moreover, the hydrophobic amino acids in purified peptides could provide more chelating spaces. This study was of great significance for the development of calcium supplement foods.Practical ApplicationCompared with inorganic calcium and organic calcium, the bioactive gelatin peptide chelated calcium has the characteristics of high utilization rate, high solubility, and high absorption rate. The raw materials are extracted from the tilapia processed waste, which reduce the cost, make full use of resources, and improve the bioavailability. The tilapia skin gelatin peptide calcium chelate can be directly absorbed by the human body, and the absorption efficiency is high, further improving the resource utilization rate and having high economic benefits, which is a comprehensive supplement that can also be used as a functional food.

Previous studies have shown that rambutan peel phenolic (RPP) extract has excellent biological activities due to its abundant phenolic content and profile. In this study, the potential anti-osteoporosis (OP) effects of RPP were evaluated by suppressing receptor activator nuclear factor-kappa B ligand (RANKL)-induced differentiation of RAW264.7 cells into osteoclasts and amelioratingretinoic acid-induced OP in rats. Our results showed that RPP efficiently decreased the formation of tartrate-resistant acid phosphatase (TRAP)-positive cells and reduced total TRAP activity in RAW264.7 cells under RANKL stimulation. RPP treatment significantlyameliorated retinoid acid-induced calcium loss in rats (p < 0.05). The serum phosphorus level of osteoporotic rats was increased by RPP treatment, and the serum levels of total alkaline phosphatase and osteocalcin in osteoporotic rats were further reduced. RPP treatment improved the qualities of the femur and tibia, such asbone mineral density, bone length, bone maximum load, cortical bone area ratio, and trabecularelative bone density in osteoporotic rats to some extent. Furthermore, histological analysis showed that RPP effectively improved the bone microstructure of osteoporotic rats by regulating the cortical bone thickness and trabecular bone separation. These results indicate that RPP could have potential applications as a newnutraceutical and functional food in the prevention of OP.