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

Research output: Contribution to journalArticlepeer-review


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

Colleges, School and Institutes

External organisations

  • Aix Marseille University
  • University of Toronto
  • Terrence Donnelly Centre for Cellular and Biomolecular Research, Toronto, Ontario, Canada.
  • University of Uppsala
  • Department for Human Genetics, Faculty of Medicine, Catholic University of Leuven, Belgium


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