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The dipeptide transporter, especially PepT1 and PepT2, are integral membrane proteins belonging to the proton-coupled oligopeptide transporter (POT) family (SLC15A subfamily), responsible for actively transporting di- and tripeptides from the intestinal lumen or renal filtrate into epithelial cells using the proton electrochemical gradient. They play a vital physiological role in protein nutrition and are notable for facilitating the uptake of a variety of clinically relevant drugs. Their structure features 12 transmembrane domains and several key residues critical for substrate and inhibitor binding. Transport is sensitive to inhibition by modified dipeptides, and conformational changes in the transporter govern substrate specificity and kinetics. Drugs targeting PepT1/2 may act as substrates or inhibitors, impacting their therapeutic efficacy and safety profile. If you require a more specific name or context (e.g., human vs. bacterial transporter), please specify, as "dipeptide transporter" can also refer to prokaryotic transporters like DtpA (E. coli), DppD (Bacillus) or others. However, in human and mammalian physiology, "dipeptide transporter" most commonly refers to PepT1 and PepT2.
Drugs are transported via proton-coupled co-transport, leveraging the proton gradient across epithelia. Competitive inhibition (e.g., some modified dipeptides act as inhibitors)
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