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)