The renal type H+/peptide symporter PEPT2: Structure-affinity relationships

A. Biegel, I. Knütter, B. Hartrodt, S. Gebauer, S. Theis, P. Luckner, G. Kottra, M. Rastetter, K. Zebisch, I. Thondorf, H. Daniel, K. Neubert, M. Brandsch

Research output: Contribution to journalArticlepeer-review

83 Scopus citations

Abstract

The H+/peptide cotransporter PEPT2 is expressed in a variety of organs including kidney, lung, brain, mammary gland, and eye. PEPT2 substrates are di- and tripeptides as well as peptidomimetics, such as β-lactam antibiotics. Due to the presence of PEPT2 at the bronchial epithelium, the aerosolic administration of peptide-like drugs might play a major role in future treatment of various pulmonary and systemic diseases. Moreover, PEPT2 has a significant influence on the in vivo disposition and half-life time of peptide-like drugs within the body, particularly in kidney and brain. PEPT2 is known to have similar but not identical structural requirements for substrate recognition and transport compared to PEPT1, its intestinal counterpart. In this review we compiled available affinity constants of 352 compounds, measured at different mammalian tissues and expression systems and compare the data whenever possible with those of PEPT1.

Original languageEnglish
Pages (from-to)137-156
Number of pages20
JournalAmino Acids
Volume31
Issue number2
DOIs
StatePublished - Aug 2006

Keywords

  • Dipeptides
  • Drug-delivery
  • Drugs
  • PEPT1
  • PEPT2
  • Peptide transport
  • Peptidomimetics
  • Tripeptides
  • β-Lactam antibiotics

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