Oxidative stress induces the formation of D-aspartyl residues in the elastin mimic peptides.
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.
Kuge
Katsunori
K
Pias Corporation, 1-3-1 Murotani Nishi-ku Kobe 651-2241, Japan.
Kitamura
Keiko
K
Nakaoji
Koichi
K
Hamada
Kazuhiko
K
Fujii
Norihiko
N
Saito
Takeshi
T
Fujii
Noriko
N
D000595:Amino Acid Sequence; D026603:D-Aspartic Acid / Q000378:metabolism*; D004549:Elastin / Q000737:chemistry / Q000378:metabolism; D018384:Oxidative Stress; D010455:Peptides / Q000737:chemistry / Q000378:metabolism* / Q000528:radiation effects; D017382:Reactive Oxygen Species / Q000378:metabolism; D013696:Temperature; D014466:Ultraviolet Rays
D010455:Peptides; D017382:Reactive Oxygen Species; D026603:D-Aspartic Acid; D004549:Elastin