Design, synthesis, and biological activity of novel triazole amino acids used to probe binding interactions between ligand and neutral amino acid transport protein SN1.
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Gajewski M, Seaver B, Esslinger CS
Design, synthesis, and biological activity of novel triazole amino acids used to probe binding interactions between ligand and neutral amino acid transport protein SN1.
Bioorg Med Chem Lett. 2007 Aug 1;17(15):4163-6. Epub 2007 May 23.
- PubMed ID
- 17561393 [ View in PubMed]
- Abstract
Novel triazole amino acids were synthesized as probes to investigate ligand-protein binding interactions of the neutral amino acid transporter SN1. The bonding hypothesis to be tested was that the side chains of endogenous substrates are acting as H-bond acceptors. Although limited inhibition of (3)H-L-glutamine uptake by SN1 expressing oocytes was observed, the synthetic compounds show a trend that suggests a hydrogen bond interaction just outside the endogenous ligand binding pocket.
DrugBank Data that Cites this Article
- Drug Transporters
Drug Transporter Kind Organism Pharmacological Action Actions L-Glutamine Sodium-coupled neutral amino acid transporter 3 Protein Humans UnknownSubstrateDetails