Dipeptide affinity and translocation relationships via the intestinal peptide transporter hPEPT1 were characterized, guiding design of peptide-based oral drugs that exploit this gut absorption pathway.
Key findingDipeptide affinity and translocation relationships via the intestinal peptide transporter hPEPT1 were characterized, guiding design of peptide-based o
What the researchers found
Dipeptide affinity and translocation relationships via the intestinal peptide transporter hPEPT1 were characterized, guiding design of peptide-based oral drugs that exploit this gut absorption pathway.
Why it matters
Relevant for peptide research.
How the study worked
research study.
What this study cannot tell us
See abstract.
How to read the evidence
emerging evidence.
When this study was published
Published in 2011.
The bigger picture
Advances peptide research.
Questions still open
- Further research needed.
Common questions
What was studied?
What was found?
Read the original research
Affinity and translocation relationships via hPEPT1 of H-X aa-Ser-OH dipeptides: evaluation of H-Phe-Ser-OH as a pro-moiety for ibuprofen and benzoic acid prodrugs.
European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V, 77(2), 327-31
Citation
Omkvist, Diana Højmark; Trangbæk, Dennis Jespersen; Mildon, Jemma; Paine, James S; Brodin, Birger; Begtrup, Mikael; Nielsen, Carsten Uhd. (2011). Affinity and translocation relationships via hPEPT1 of H-X aa-Ser-OH dipeptides: evaluation of H-Phe-Ser-OH as a pro-moiety for ibuprofen and benzoic acid prodrugs.. European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V, 77(2), 327-31. https://doi.org/10.1016/j.ejpb.2010.12.009