Amino Acids · 2021 · 112 citations · 104 references
Life SciencesBiochemistryFood ScienceFood ChemistryPost-translational ModificationProtein BiochemistryLipid OxidationOxidative Damage To BiomoleculesProtein ChemistryProtein MetabolismProtein OxidationProteins In FoodsCarbonylation ReactionsMalondialdehyde AdductsMalondialdehyde FormationOxidative Damage In ProteinsOxidative Protein DamageProtein AggregatesProtein PeroxidationRedox Post-translational Modifications
Protein oxidation is a topic of indisputable scientific interest given the impact of oxidized proteins on food quality and safety. Carbonylation is regarded as one of the most notable post-translational modifications in proteins and yet, this reaction and its consequences are poorly understood. From a mechanistic perspective, primary protein carbonyls (i.e. α-aminoadipic and γ-glutamic semialdehydes) have been linked to radical-mediated oxidative stress, but recent studies emphasize the role alternative carbonylation pathways linked to the Maillard reaction. Secondary protein carbonyls are introduced in proteins via covalent linkage of lipid carbonyls (i.e. protein-bound malondialdehyde). The high reactivity of protein carbonyls in foods and other biological systems indicates the intricate chemistry of these species and urges further research to provide insight into these molecular mechanisms and pathways. In particular, protein carbonyls are involved in the formation of aberrant and dysfunctional protein aggregates, undergo further oxidation to yield carboxylic acids of biological relevance and establish interactions with other biomolecules such as oxidizing lipids and phytochemicals. From a methodological perspective, the routine dinitrophenylhydrazine (DNPH) method is criticized not only for the lack of accuracy and consistency but also authors typically perform a poor interpretation of DNPH results, which leads to misleading conclusions. From a practical perspective, the biological relevance of protein carbonyls in the field of food science and nutrition is still a topic of debate. Though the implication of carbonylation on impaired protein functionality and poor protein digestibility is generally recognized, the underlying mechanism of such connections requires further clarification. From a medical perspective, protein carbonyls are highlighted as markers of protein oxidation, oxidative stress and disease. Yet, the specific role of specific protein carbonyls in the onset of particular biological impairments needs further investigations. Recent studies indicates that regardless of the origin (in vivo or dietary) protein carbonyls may act as signalling molecules which activate not only the endogenous antioxidant defences but also implicate the immune system. The present paper concisely reviews the most recent advances in this topic to identify, when applicable, potential fields of interest for future studies.
104
Age-related changes in oxidized proteins.
Cynthia N. Oliver, Byungchan Ahn, Elena J. Moerman et al. · Journal of Biological Chemistry · 1987 · 1.3K citations · Full text
Advances in Food and Nutrition Research
Carol A. Friesen · Journal of Nutrition Education and Behavior · 2017 · 525 citations
Agriculture, Food Science, Nutrition +12
2-Aminoadipic acid is a biomarker for diabetes risk
Thomas J. Wang, Debby Ngo, Nikolaos Psychogios et al. · Journal of Clinical Investigation · 2013 · 468 citations · Full text