Hidden route of protein damage through oxygen-confined photooxidation.

Seoyoon Kim, Eojin Kim, Mingyu Park, Seong Ho Kim, Byung-Gyu Kim, Seungjin Na, Victor W Sadongo, W C Bhashini Wijesinghe, Yu-Gon Eom, Gwangsu Yoon, Hannah Jeong, Eunhye Hwang, Chaiheon Lee, Kyungjae Myung, Chae Un Kim, Jeong-Mo Choi, Seung Kyu Min, Tae-Hyuk Kwon, Duyoung Min

Department of Chemistry, Ulsan National Institute of Science and Technology, Ulsan, 44919, Republic of Korea. · pubmed

Paper

Abstract

Oxidative modifications can disrupt protein folds and functions, and are strongly associated with human aging and diseases. Conventional oxidation pathways typically involve the free diffusion of reactive oxygen species (ROS), which primarily attack the protein surface. Yet, it remains unclear whether and how internal protein folds capable of trapping oxygen (O

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Research summary

The paper addresses oxidative modifications of proteins, which are linked to aging and age-related diseases. However, it primarily focuses on the mechanisms of protein damage rather than proposing solutions to mitigate or reverse aging processes. The findings may contribute to understanding the underlying biology of aging, but they do not present a significant advancement or breakthrough in longevity research.

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