Techniques to decipher molecular diversity by phage display

Dawn R. Christiansen, Michael G. Ozawa, Renata Pasqualini, Wadih Arap

Research output: Chapter in Book/Report/Conference proceedingChapter

30 Scopus citations


Combinatorial phage display technology may be applied to decipher the molecular diversity of peptide binding specificity to isolated proteins, purified antibodies, cell surfaces, intracellular/cyto-domains, and blood vessels in vivo. The application of such a strategy ranges from identifying receptor-ligand pairs and antigen binding sites to understanding the progression of diseases by their differential expression patterns and developing therapeutic targeting strategies. Different strategies can be used to isolate peptides from diverse libraries displayed on the surface of bacteriophage by exposing the library to a target molecule or organ, washing away nonbinding phage, eluting and amplifying the bound phage for multiple round use, and then analyzing the peptide sequences of the enriched phage. The following methods first outline the construction of a phage library and then delineate various in vitro and in vivo biopanning applications to probe isolated integrins, purified antibodies, cell surface molecules, and vascular endothelial cells.

Original languageEnglish (US)
Title of host publicationCardiovascular Proteomics
Subtitle of host publicationMethods and Protocols
EditorsFernando Vivanco
Number of pages22
StatePublished - Feb 5 2007
Externally publishedYes

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics


  • Angiogenesis
  • Antibody fingerprinting
  • Biopanning
  • Molecular markers
  • Phage display
  • Protein
  • Vascular targeting


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