Drug and peptide transport in humans

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Revision as of 01:05, 4 December 2024

This page is under construction. This notice will be removed when it is ready. Eric Martz 01:56, 3 December 2024 (UTC)

↑ ^1.0 ^1.1 Killer M, Wald J, Pieprzyk J, Marlovits TC, Low C. Structural snapshots of human PepT1 and PepT2 reveal mechanistic insights into substrate and drug transport across epithelial membranes. Sci Adv. 2021 Nov 5;7(45):eabk3259. doi: 10.1126/sciadv.abk3259. Epub 2021 Nov 3. PMID:34730990 doi:http://dx.doi.org/10.1126/sciadv.abk3259
↑ Shen J, Hu M, Fan X, Ren Z, Portioli C, Yan X, Rong M, Zhou M. Extracellular domain of PepT1 interacts with TM1 to facilitate substrate transport. Structure. 2022 Jul 7;30(7):1035-1041.e3. PMID:35580608 doi:10.1016/j.str.2022.04.011

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 <StructureSection load='' size='350' side='right' caption='' scene='10/1066775/Chimerax-morph-pdb/2'>
 ==Peptide Transporter Function & Structure==
-Human peptide transporter 1 ('''PepT1''') plays a crucual role in nutrition, transporting peptides from digested protein into intestinal cells.<ref name="kl">PMID: 34730990</ref> It is also crucial in uptake of orally delivered drugs.
+Human promiscuous peptide transporter 1 ('''PepT1''') plays a crucual role in nutrition, transporting di- and tri-peptides from digested protein into intestinal cells.<ref name="kl">PMID: 34730990</ref> It is also crucial in uptake of orally delivered drugs.<ref name="kl" /> PepT1 is a 708-amino acid protein with an extracellular domain (beta sheets), a transmembrane transporter domain (alpha helices), and an amphipathic 2-helix cytoplasmic linker (green protrusion). The latter looks like the '''toe of a boot''' formed by the linker (toe) with the transmembrane domain. The function of the cytoplasmic and linker domains are not well understood, although the cytoplasmic domain appears to be important in transport<ref name="cytodom">PMID: 35580608</ref>.
 <scene name='10/1066775/7pmx/1'>7pmx cartoon</scene>