Beta- and gamma-di- and tripeptides as potential substrates for the oligopeptide transporter hPepT1.
The hPepT1-mediated transport properties of a series of 11 synthesized beta- and gamma-peptides have been studied in Caco-2 cells. The results show that several of the compounds interact with the peptide transporter, but only two beta-dipeptides act as substrates and are transported across the cell monolayers. These two are less-efficient substrates than alpha-peptides. Larger derivatives than beta-dipeptides do not act as hPepT1 substrates, but instead, they appear to be substrates for P-glycoprotein efflux.
Hubatsch
Ina
I
Department of Pharmacy, Uppsala University, Box 580, SE-751 23 Uppsala, Sweden. ina.hubatsch@farmaci.uu.se
Arvidsson
Per I
PI
Seebach
Dieter
D
Luthman
Kristina
K
Artursson
Per
P
D020168:ATP Binding Cassette Transporter, Subfamily B, Member 1 / Q000378:metabolism; D001693:Biological Transport, Active; D018938:Caco-2 Cells; D002463:Cell Membrane Permeability; D004151:Dipeptides / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D007413:Intestinal Mucosa / Q000378:metabolism; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism; D000074011:Peptide Transporter 1; D013329:Structure-Activity Relationship; D027981:Symporters / Q000378:metabolism*
D020168:ATP Binding Cassette Transporter, Subfamily B, Member 1; D004151:Dipeptides; D009842:Oligopeptides; D000074011:Peptide Transporter 1; C082186:SLC15A1 protein, human; D027981:Symporters