Thermo-stable nature of aromatic monoamine-dependent superoxide-generating activity of human prion-derived Cu-binding peptides

Biosci Biotechnol Biochem. 2009 May;73(5):1218-20. doi: 10.1271/bbb.90012. Epub 2009 May 7.

Abstract

Human prion protein has four distinct Cu-binding motifs that catalyze the generation of superoxide coupled to oxidation of phenols and amines. Here, the thermostability of the superoxide-generating prion-derived peptides was tested. Among the peptides tested, two maintained high catalytic activity even after heating and repeated freezing/thawing cycles. The biological roles for these thermostable catalysts are discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amines / chemistry
  • Amines / metabolism*
  • Amino Acid Sequence
  • Animals
  • Cattle
  • Copper / metabolism*
  • Humans
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Peptides / metabolism*
  • Prions / chemistry*
  • Protein Stability
  • Superoxides / metabolism*
  • Temperature

Substances

  • Amines
  • Peptides
  • Prions
  • Superoxides
  • Copper