The immunosuppressive activity and solution structures of ubiquitin fragments

Łukasz Jaremko, Mariusz Jaremko, Paweł Pasikowski, Marek Cebrat, Piotr Stefanowicz, Marek Lisowski, Jolanta Artyin, Michał Zimecki, Igor Zhukov, Zbigniew Szewczuk

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


Recently, ubiquitin was suggested as a promising antiinflammatory protein therapeutic. We found that a peptide fragment corresponding to the ubiquitin50-59 sequence (LEDGRTLSDY) possessed the immunosuppressive activity comparable with that of ubiquitin. CD and NMR spectroscopies were used to determine the conformational preferences of LEDGRTLSDY in solution. The peptide mixture, obtained by pepsin digestion of ubiquitin, was even more potent than the intact protein. Although the peptide exhibited a well-defined conformation in methanol, its structure was distinct from the corresponding 50-59 fragment in the native ubiquitin molecule.

Original languageEnglish (US)
Pages (from-to)423-431
Number of pages9
Issue number6
StatePublished - 2009
Externally publishedYes


  • Cryptides
  • Immunomodulation
  • NMR
  • Peptic fragments
  • Retro-RGD sequence
  • Solution structure
  • Ubiquitin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Biomaterials
  • Organic Chemistry


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