Oxidative stress induces the formation of D-aspartyl residues in the elastin mimic peptides

Chem Biodivers. 2010 Jun;7(6):1408-12. doi: 10.1002/cbdv.200900348.

Abstract

Racemization of aspartyl (Asp) residues in peptides and proteins has been considered to be a nonenzymatic chemical reaction which occurs via succinimide formation. However, it has not been known yet what conditions in living body accelerate the inversion of the L- to the D-form. Here, we examined the effect of ultraviolet (UV) exposure or oxidative stress on the formation of D-Asp residues in the elastin mimic peptides with or without heat treatment. As a result, UV exposure did not affect the D-Asp formation in peptides. On the other hand, the amount of D-Asp in heat-treated peptide solution at the same time as addition of HO(.) radical, H(2)O(2), and lipid peroxide was significantly increased. These results indicate that the inversion rate to D-form of Asp residues in skin elastin is accelerated by generation of reactive oxygen species (ROS), and that oxidative stress might be closely related to D-Asp formation in aging proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • D-Aspartic Acid / metabolism*
  • Elastin / chemistry
  • Elastin / metabolism
  • Oxidative Stress*
  • Peptides / chemistry
  • Peptides / metabolism*
  • Peptides / radiation effects
  • Reactive Oxygen Species / metabolism
  • Temperature
  • Ultraviolet Rays

Substances

  • Peptides
  • Reactive Oxygen Species
  • D-Aspartic Acid
  • Elastin