Products Cited in Publications Worldwide The Prototypical Oligopeptide Transporter YdgR From E. coli Exhibits a Strict Preference for β‐Ala‐Lys (AMCA)

The Prototypical Oligopeptide Transporter YdgR From E. coli Exhibits a Strict Preference for β‐Ala‐Lys (AMCA)

Sajid, Salvia; Ninh, Cecilia; Yan, Ruyu; Rafiq, Maria; Christensen, Lars Porskjær; Jørgensen, Mikkel Girke; Hansen, Paul Robert; Franzyk, Henrik; Mirza, Osman; Prabhala, Bala Krishna

DOI: PMID:

Abstract

Fluorescent probes are widely used in cellular imaging and disease diagnosis. Acting as substitute carriers, fluorescent probescan also be used to help transport drugs within cells. In this study, commonly used fluorophores, TAMRA (), PBA (), NBD (nitrobenzoxadiazole), OG (Oregon Green), and CF ()were conjugated with the dipeptide β-Ala-Lys, the peptide moiety of the well-established peptide transporter substrate β-Ala-Lys(AMCA) (AMCA: 7-amino- 4-methyl-coumarin-3-acetic acid) by modifying it with respect to side-chain length and func-tional end groups. The analogs were tested for transport through or inhibition of YdgR, a prototypical peptide transporter fromE. coli and apparently homologous to the human PEPT1. Strikingly, none of the dipeptide-fluorophore conjugates nor minormodifications in the reporter substrate were tolerated by YdgR, indicating discrepancies to PEPT1. These findings underscoreintricate substrate recognition mechanisms governing substrate recognition by YdgR.

Keywords

fluorophores ; uptake assays ; YdgR ; β-Ala-Lys(AMCA)

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Boc-β-N-Me-Ala-OH

A118650124072-61-397%

Boc-β-N-Me-Ala-OH

10.0/250mg

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