The immunosuppressive activity and solution structures of ubiquitin fragments

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

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
JournalBiopolymers
Volume91
Issue number6
DOIs
StatePublished - Aug 3 2009

Keywords

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

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry

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