10.1002/cbic.201000759
The research presents an in-depth study on the transport of free and peptide-bound glycated amino acids, focusing on their synthesis, transepithelial flux across Caco-2 cell monolayers, and interactions with apical membrane transport proteins. The experiments involved the synthesis of various glycated amino acids and dipeptides through non-enzymatic chemical processes known as the Maillard reaction, using reactants like lysine, arginine, glucose, and other sugars. The synthesized products were analyzed using techniques such as high-pressure liquid chromatography (HPLC), amino acid analysis (AAA), nuclear magnetic resonance (NMR) spectroscopy, mass spectrometry, and elemental analysis. The study also measured the inhibition of lysine and glycylsarcosine uptakes in Caco-2 cells, which express transporters like PEPT1 and lysine transport systems, to understand the affinities and transport characteristics of these glycated compounds. The results provided insights into the intestinal absorption mechanisms of dietary Maillard reaction products and their potential impact on human health.
