Proteomic peptide phage display uncovers novel interactions of the PDZ1-2 supramodule of syntenin

Sarah Garrido-Urbani, Pankaj Garg, Rania Ghossoub, Frédérique Lembo, Gustav N Sundell, Philip M Kim, Marc Lopez, Pascale Zimmermann, Sachdev S Sidhu, Ylva Ivarsson, Roland Arnold

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)
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Syntenin has crucial roles in cell adhesion, cell migration and synaptic transmission. Its closely linked postsynaptic density-95, discs large 1, zonula occludens-1 (PDZ) domains typically interact with C-terminal ligands. We profile syntenin PDZ1-2 through proteomic peptide phage display (ProP-PD) using a library that displays C-terminal regions of the human proteome. The protein recognizes a broad range of peptides, with a preference for hydrophobic motifs and has a tendency to recognize cryptic internal ligands. We validate the interaction with nectin-1 through orthogonal assays. The study demonstrates the power of ProP-PD as a complementary approach to uncover interactions of potential biological relevance.

Original languageEnglish
Pages (from-to)3-12
Number of pages10
JournalFEBS Letters
Issue number1
Early online date8 Jan 2016
Publication statusPublished - Jan 2016


  • Amino Acid Motifs
  • Animals
  • Binding Sites
  • COS Cells
  • Cell Adhesion Molecules
  • Cercopithecus aethiops
  • Computational Biology
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Immobilized Proteins
  • Kinetics
  • Ligands
  • MCF-7 Cells
  • Models, Molecular
  • Nectins
  • PDZ Domains
  • Peptide Fragments
  • Peptide Library
  • Proteomics
  • Recombinant Proteins
  • Syntenins
  • Two-Hybrid System Techniques
  • Journal Article
  • Research Support, Non-U.S. Gov't
  • Validation Studies


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