Redox Report

Recent Developments in Protein Oxidation

Proteins, often called the workhorses of cells due to the many roles that these fulfil (e.g. structure, signalling, enzymes). As a result of their very high abundance (billions of proteins per cell) and the presence of electron-rich sidechains, proteins are very susceptible to modification by oxidants arising from cellular processes (e.g. peroxides, hypohalous acids, peroxynitrite, etc) and external factors (e.g. pollutants, UV light, etc). Depending on the modification site, the reversibility of the products, and the abundance of such modifications, these alterations can have major impacts at both a structural and functional level with implications for physiology and pathology.

The oxidative (bio)chemistry of proteins is very complex. While reversible modifications at specific residues are essential for some biological processes and functions (e.g. cell signalling), accumulation of oxidative damage and formation of irreversible products on proteins can be a cause, or a result, of tissue dysfunction and disease progression (e.g. cardiovascular, inflammation, neurodegenerative conditions, cancer, etc). Therefore, determining whether, how and when oxidative damage occurs on proteins, in a quantitative and rigorous manner, is key to allow the rational and informed development of biomedical and technological strategies to prevent oxidative damage and disease progression.

This Article collection, entitled “Recent Developments in Protein Oxidation”, aims to present a collection of original research articles and reviews, highlighting recently elucidated mechanisms of protein modification, the structural and functional consequences of protein oxidation, and also methodological advances to determine and quantify oxidized proteins. This collection will be an important resource for chemists, biochemists, cell biologists and clinicians interested in processes concerning the oxidative biology of proteins in health and disease.

5 Keywords:

1. Protein oxidation
2. Oxidative stress
3. Post-translational modification
4. Cell signalling
5. Protein cross-linking

Guest Advisors:

Dr. Eduardo Fuentes-Lemus received his PhD in Chemistry in 2018, and since 2024 is Assistant Prof. at the Pontifical Catholic University of Chile (Chile). His current research interests include understanding different physicochemical aspects that modulate protein oxidation and glycation, particularly the effect that biological interfaces, crowding and microdomains would have on the pathways and kinetics of protein modification. For further details about Dr. Fuentes-Lemus's professional profile, kindly refer to these links: https://quimica.uc.cl/investigacion/academicos/eduardo-fuentes-l/, https://orcid.org/0000-0002-1465-8466.

Professor Michael Davies has approximately 40 years of experience in the field of protein oxidation and modification. His research group have contributed significantly to understanding mechanisms of protein alteration induced by a wide range of different oxidants, and the detection and quantification of products, both in vitro and in vivo. He has a particular focus on linking basic biochemical mechanisms to clinical information and patient outcomes. For further details about Prof. Davies's professional profile, kindly refer to these links: https://bmi.ku.dk/english/research/inflammation-metabolism-and-oxidation/davies-group/, https://orcid.org/0000-0002-5196-6919.

Disclosure Statement: Guest Advisors have no conflicts of interest to disclose.

Please review the journal scope and author submission instructions prior to submitting a manuscript.

To submit your papers to this Article Collection, please:

1. Check "yes" for the question, "Are you submitting your paper for a specific special issue or article collection?"
2. Select the Article Collection "Recent Developments in Protein Oxidation" from the drop-down menu under the question, "Special Issue or Article Collection Name."

Please contact Changluan Zhou at [email protected] with any queries and discount codes regarding this Article Collection.