glutamylalanine has been researched along with glycylsarcosine* in 1 studies
1 other study(ies) available for glutamylalanine and glycylsarcosine
Article | Year |
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Application of enzymatically stable dipeptides for enhancement of intestinal permeability. Synthesis and in vitro evaluation of dipeptide-coupled compounds.
Transport across the intestinal barrier of compounds with low permeability may be facilitated by targeting the human oligopeptide transporter, hPepT1. A flexible synthetic pathway for attaching compounds to dipeptides through ester or amide bonds was developed. Furthermore, a synthetic approach to functionalize model drugs from one key intermediate was generated and applied to a glucose-6-phosphatase active model drug. The model drug was coupled to D-Glu-Ala through various linkers, and the G-6-Pase activity as well as the aqueous solubility and transport properties of these prodrugs, as compared to those of the parent drugs, were examined. None of the peptide-coupled compounds seemed to be transported by hPepT1, though one of the peptide-coupled compounds had affinity for hPepT1. Interestingly, in one case the parent drug was actively effluxed, while the corresponding peptide-coupled prodrug was not. The low aqueous solubility of the parent compounds was not increased after attachment to a dipeptide. This suggests that only compounds with a certain intrinsic aqueous solubility should be targeted to hPepT1 by attachment to a dipeptide. Important information about the design of peptide-coupled drugs targeted for hPepT1 is presented. Topics: Benzyl Alcohols; Biological Transport, Active; Caco-2 Cells; Cadherins; Carrier Proteins; Dipeptides; Drug Design; Drug Stability; Enzyme Inhibitors; Glucose-6-Phosphatase; Humans; Hydrogen-Ion Concentration; Jejunum; Kinetics; Membrane Transport Proteins; Models, Chemical; Peptide Transporter 1; Permeability; Prodrugs; Quantitative Structure-Activity Relationship; Symporters; Tumor Cells, Cultured | 2001 |