Characterization of linear mimetic peptides of Interleukin-22 from dissection of protein interfaces

Sara La Manna, Pasqualina Liana Scognamiglio, Concetta Di Natale, Marilisa Leone, Flavia Anna Mercurio, Anna Maria Malfitano, Francesca Cianfarani, Stefania Madonna, Sergio Caravella, Cristina Albanesi, Ettore Novellino, Daniela Marasco

Research output: Contribution to journalArticlepeer-review


Interleukin-22 (IL-22) belongs to the family of IL-10 cytokines and is involved in a wide number of human diseases, including inflammatory disorders and cancer pathology. The ligand-receptor complex IL-22/IL-22R plays a key role in several pathways especially in the regulation and resolution of immune responses. The identification of novel compounds able to modulate IL-22/IL-22R complex could open the route to new therapeutic strategies in multiple human diseases. In this study, we designed and characterized IL-22 derived peptides at protein interface regions: several sequences revealed able to interfere with the protein complex with IC50 in the micromolar range as evaluated through Surface Plasmon Resonance (SPR) experiments. Their conformational characterization was carried out through Circular Dichroism (CD) and Nuclear Magnetic Resonance (NMR) spectroscopies, shedding new light into the features of IL-22 fragments and on structural determinants of IL-22/IL-22R1 recognition. Finally, several peptides were tested on human keratinocyte cultures for evaluating their ability to mimic the activation of molecular pathways downstream to IL-22R in response to IL-22 binding.

Original languageEnglish
Pages (from-to)106-115
Number of pages10
Publication statusPublished - Jul 1 2017


  • Circular dichroism
  • IL-22 signalling
  • Interface protein regions

ASJC Scopus subject areas

  • Biochemistry


Dive into the research topics of 'Characterization of linear mimetic peptides of Interleukin-22 from dissection of protein interfaces'. Together they form a unique fingerprint.

Cite this