The immunosuppressive activity and solution structures of ubiquitin fragments

Biopolymers. 2009 Jun;91(6):423-31. doi: 10.1002/bip.21160.

Abstract

Recently, ubiquitin was suggested as a promising anti-inflammatory protein therapeutic. We found that a peptide fragment corresponding to the ubiquitin(50-59) 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. (c) 2009 Wiley Periodicals, Inc. Biopolymers 91: 423-431, 2009.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cells, Cultured
  • Circular Dichroism
  • Immunosuppressive Agents / chemistry
  • Immunosuppressive Agents / pharmacology*
  • Magnetic Resonance Spectroscopy
  • Mass Spectrometry
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Pepsin A / chemistry
  • Peptide Fragments*
  • Sheep
  • Solutions / chemistry
  • Ubiquitin / chemistry
  • Ubiquitin / pharmacology*

Substances

  • Immunosuppressive Agents
  • Peptide Fragments
  • Solutions
  • Ubiquitin
  • Pepsin A