Earthworms have been a traditional medicine in China for at least 2300 years. Because of medicine food homology in China, people have been using earthworms as a food for several centuries. Earthworms are rich in protein and various amino acids; the protein content of earthworm meal was 54.6-59.4% on dry weight. Their protein content and amino acid composition are beter than those of ish meal, cow milk and soybean meal. The crude fat content of earthworm meal was 7.34%. Earthworm protein is easily hydrolyzed into free amino acids. The hydrolyzed body luids contain 9.34% protein and 78.73 mg of free amino acids per liter of raw luid and are rich in vitamins and minerals. By the fast development of molecular biological techniques, more Verm pharmaceuticals and functional components were isolated from earthworms. An antibacterial peptide and a functional earthworm powder were introduced in this paper. In short, based on its nutrient content and functional components, earthworms could be an excellent raw material source as homology of medicine and food for human use, especially as functional food in the future.

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One of the major challenges for discovering protein-protein interaction inhibitors is identifying selective and druggable binding sites at the protein surface. Here, we report an approach to identify a small molecular binding site to selectively inhibit the interaction of soluble RANKL and RANK for designing anti-osteoporosis drugs without undesirable immunosuppressive effects. Through molecular dynamic simulations, we discovered a binding site that allows a small molecule to selectively interrupt soluble RANKL-RANK interaction and without interfering with the membrane RANKL-RANK interaction. We describe a highly potent inhibitor, S3-15, and demonstrate its specificity to inhibit the soluble RANKL-RANK interaction with in vitro and in vivo studies. S3-15 exhibits anti-osteoporotic effects without causing immunosuppression. Through in silico and in vitro experiments we further confirm the binding model of S3-15 and soluble RANKL. This work might inspire structure-based drug discovery for targeting protein-protein interactions.

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