In some cases Metformin (MF) produces intestinal discomfort and increased risk of dysbiosis. We developed a novel astragalus compound oral solution (termed "OS") and investigated effects of treatments with OS alone or in combination with metformin (MF) in a type 2 diabetes (T2D) mouse model. OS can treat T2D in mice. OS, in comparison with MF (OS + MF), was more effective in improving HDL, ALT, hepatic glycogen, and GSH-px levels, and in protecting several organs simultaneously. Gut microbiota composition and diversity were significantly better for OS and OS + MF than for MF. Helicobacter, Oscillospira, Mucispirillum, Dehalobacterium, Anaerotruncus, Subdoligranulum, Akkermansia, Allobaculum, and Ochrobactrum were significantly correlated with FBG, liver function indicators, and islet cell areas. Our findings suggest that OS applied in combination with MF promoted health in the T2D mouse model through effects on 192 related targets to regulate glucose and lipid metabolism, protect organs, and improve gut microbiota composition
Celiac disease (CD) is a prevalent disorder with autoimmune features. Dietary exposure of wheat gluten (including gliadins and glutenins) to the small intestine activates the gluten-reactive CD4+ T cells and controls the disease development. While the human leukocyte antigen (HLA) is the single most important genetic factor of this polygenic disorder, HLA-DQ2 recognition of gluten is the major biological step among patients with CD. Gluten epitopes are often rich in Pro and share similar primary sequences. Here, we simulated the solution structures changes of a variety of gluten epitopes under different pH and temperatures, to mimic the fermentation and baking/cooking processes. Based on the crystal structure of HLA-DQ2, binding of differently processed gluten epitopes to DQ2 was studied in silico. This study revealed that heating and pH change during the fermentation process impact the solution structure of gluten epitope. However, binding of differently treated gluten epitope peptide (GEP) to HLA-DQ2 mainly depended on its primary amino acid sequence, especially acidic amino acid residues that play a pivotal role in their recognition by HLA-DQ2.
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