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Two new studies from Associate Professor Simon Newstead in the Department of Biochemistry reveal how a family of membrane proteins that enable us to absorb protein in our food can transport thousands of different peptide fragment into cells.

Lipid Cubic Phase crystallisation of bacterial POT family transporters has revealed key insights into the peptide binding site
Lipid Cubic Phase crystallisation of bacterial POT family transporters has revealed key insights into the peptide binding site

The work of Professor Newstead and colleagues, which combines high-resolution structural studies and thermodynamics, reveals the tricks that the transporters use to accomplish this promiscuity (1,2). They show that a bacterial version of the transporter, PepT1, uses different mechanisms to accommodate and transport a diverse range of peptides. If the human peptide transporter also uses two mechanisms, then companies who are interested in exploiting the transporters’ ability to actively take up a number of clinically important drugs such as antibiotics and antivirals, could hone their strategy for targeting these transporters for drug uptake.

Read more (Department of Biochemistry website)

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