Application of Phage Display for Ligand Peptidomics to Identify Peptide Ligands Binding to AQP2-Expressing Membrane Fractions

  • Byung-Heon Lee
  • Tae-Hwan Kwon
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 1023)

Abstract

In vitro phage display represents an emerging and innovative technology for the rapid isolation of high-affinity peptide ligands. Phage display technologies using phages comprising a vast library of peptides have become fundamental to the isolation of high-affinity binding ligands for diagnostic and therapeutic applications, e.g., ligand proteomics, discovery of novel protein–protein interactions, antibody engineering, targeted delivery of therapeutic agents, and development of imaging probes. This chapter describes the procedures for phage display selection of peptide ligands that selectively bind to aquaporin-2-expressing membrane fractions of rat kidney.

Key words

Aquaporin Collecting duct Ligand peptidomics In vitro phage display Vasopressin 

Notes

Acknowledgements

This study was supported by National Research Foundation grant funded by the Ministry of Education, Science and Technology (MEST), Korea (2010-0008225 and 2010-0019393).

References

  1. 1.
    Knepper MA, Nielsen S, Chou CL, DiGiovanni SR (1994) Mechanism of vasopressin action in the renal collecting duct. Semin Nephrol 14:302–321PubMedGoogle Scholar
  2. 2.
    Kwon TH, Nielsen J, Møller HB, Fenton RA, Nielsen S, Frøkiaer J (2009) Aquaporins in the kidney. Handb Exp Pharmacol 190:95–132Google Scholar
  3. 3.
    Nielsen S, Frokiaer J, Marples D, Kwon TH, Agre P, Knepper MA (2002) Aquaporins in the kidney: from molecules to medicine. Physiol Rev 82:205–244PubMedGoogle Scholar
  4. 4.
    Valenti G, Procino G, Tamma G, Carmosino M, Svelto M (2005) Minireview: aquaporin 2 trafficking. Endocrinology 146:5063–5070PubMedCrossRefGoogle Scholar
  5. 5.
    Marples D, Knepper MA, Christensen EI, Nielsen S (1995) Redistribution of aquaporin-2 water channels induced by vasopressin in rat kidney inner medullary collecting duct. Am J Physiol 269:C655–C664PubMedGoogle Scholar
  6. 6.
    Rojek A, Fuchtbauer EM, Kwon TH, Frokiaer J, Nielsen S (2006) Severe urinary concentrating defect in renal collecting duct-selective AQP2 conditional-knockout mice. Proc Natl Acad Sci USA 103:6037–6042PubMedCrossRefGoogle Scholar
  7. 7.
    Lee YJ, Choi HJ, Lim JS, Earm JH, Lee BH, Kim IS, Frokiaer J, Nielsen S, Kwon TH (2008) A novel method of ligand peptidomics to identify peptide ligands binding to AQP2-expressing plasma membranes and intracellular vesicles of rat kidney. Am J Physiol Renal Physiol 295:F300–F309PubMedCrossRefGoogle Scholar
  8. 8.
    Lee SM, Lee EJ, Hong HY, Kwon MK, Kwon TH, Choi JY, Park RW, Kwon TG, Yoo ES, Yoon GS, Kim IS, Ruoslahti E, Lee BH (2007) Targeting bladder tumor cells in vivo and in the urine with a peptide identified by phage display. Mol Cancer Res 5:11–19PubMedCrossRefGoogle Scholar
  9. 9.
    Hong HY, Lee HY, Kwak W, Yoo J, Na MH, So IS, Kwon TH, Park HS, Huh S, Oh GT, Kwon IC, Kim IS, Lee BH (2008) Phage display selection of peptides that home to atherosclerotic plaques: IL-4 receptor as a candidate target in atherosclerosis. J Cell Mol Med 12:2003–2014PubMedCrossRefGoogle Scholar
  10. 10.
    Lee YJ, Song IK, Jang KJ, Nielsen J, Frokiaer J, Nielsen S, Kwon TH (2007) Increased AQP2 targeting in primary cultured IMCD cells in response to angiotensin II through AT1 receptor. Am J Physiol Renal Physiol 292:F340–F350PubMedCrossRefGoogle Scholar
  11. 11.
    Azzazy HM, Highsmith WE Jr (2002) Phage display technology: clinical applications and recent innovations. Clin Biochem 35:425–445PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  • Byung-Heon Lee
    • 1
  • Tae-Hwan Kwon
    • 1
  1. 1.Department of Biochemistry and Cell Biology, School of MedicineKyungpook National UniversityTaeguSouth Korea

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