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Postgraduate Research :
Members of the proton-coupled oligopeptide transporter (POT) family are responsible for transporting small peptides across the cell membrane. The mammalian PepT1 and PepT2 transporters play a key role in this process for dietary peptide uptake in the small intestine and peptide retention in kidney, respectively, and are capable of recognizing and transporting a diverse library (~8000 combinations) of di- and tri-peptides. Recently, PepT1 has also been shown to transport drugs with peptide-like structures, such as β-lactam antibiotics. This makes PepT1 and PepT2 attractive targets to improve drug uptake and bioavailability within the body.
My work focuses on the functional dynamics of PepTso, a bacterial homologue of PepT1. Given the high substrate promiscuity of these peptide transporters, the binding site must be incredibly accommodating and flexible in order to recognize and transport various substrates. Using solid-state NMR, electron spin resonance, and other biophysical techniques, I will examine the conformational changes of PepTso in lipid bilayer during peptide transport and gain insight into the molecular environment for substrate recognition. This information will be invaluable for future drug designs to improve drug recognition and transport by PepT1 and PepT2.
Page Last Updated: 04/11/2016 by Claudia Cassidy
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