Oxidative Stress Induces the Formation of D-Aspartyl Residues in the Elastin Mimic Peptides

✍ Scribed by Katsunori Kuge; Keiko Kitamura; Koichi Nakaoji; Kazuhiko Hamada; Norihiko Fujii; Takeshi Saito; Noriko Fujii

• Publisher: John Wiley and Sons
• Year: 2010
• Tongue: English
• Weight: 154 KB
• Volume: 7
• Category: Article
• ISSN: 1612-1872
• DOI: 10.1002/cbdv.200900348

✦ Synopsis

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.