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http://dx.doi.org/10.1073/pnas.1717373114 | DOI Listing |
Angew Chem Int Ed Engl
January 2025
University of Regensburg, Faculty of Chemistry and Pharmacy, Institute of Inorganic Chemistry, Universitätsstraße 31, D-93053, Regensburg, GERMANY.
Aminophosphates are the focus of research on prebiotic phosphorylation chemistry. Their bifunctional nature also makes them a powerful class of organocatalysts. However, the structural chemistry and dynamics of proton-binding in phosphorylation and organocatalytic mechanisms are still not fully understood.
View Article and Find Full Text PDFFood Funct
January 2025
School of Food and Biological Engineering, Jiangsu University, Zhenjiang, China.
A previous study has revealed that () dy-1 fermentation changed the structural properties and fecal fermentation characteristics of barley dietary fiber. However, the health-promoting effects of fermented dietary fiber remained unclear. This study was aimed at comparing the ameliorative effects of barley dietary fiber fermented with or without dy-1 on lipid metabolism, gut microbiota composition and hepatic energy metabolism.
View Article and Find Full Text PDFEur J Nutr
November 2024
Institute of in vivo and in vitro Models, University of Veterinary Medicine Vienna, Veterinärplatz 1, 1210, Vienna, Austria.
Purpose: Necrotizing enterocolitis (NEC) is the most severe gastrointestinal disease in preterm infants caused by an exaggerated intestinal epithelial immune activation. Several studies show that modulation of toll-like receptor 9 (TLR9) activity may have positive effects on preventing intestinal inflammatory mechanisms ultimately resulting in NEC development. In this study, the effect of various infant formulas (IF) and the probiotic strain Limosilactobacillus fermentum CECT5716 on TLR9 activation were analyzed in vitro.
View Article and Find Full Text PDFAstrobiology
December 2024
Earth-Life Science Institute, Institute of Science Tokyo, Tokyo, Japan.
Nat Commun
October 2024
Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República, 2780-157, Oeiras, Portugal.
Liquid-liquid phase separation (LLPS) in living cells provides innovative pathways for synthetic compartmentalized catalytic systems. While LLPS has been explored for enhancing enzyme catalysis, its potential application to catalytic peptides remains unexplored. Here, we demonstrate the use of coacervation, a key LLPS feature, to constrain the conformational flexibility of catalytic peptides, resulting in structured domains that enhance peptide catalysis.
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