Thiol oxidation in glycation context

Thiol oxidation in the context of glycation refers to the oxidative modification of protein sulfhydryl (-SH) groups, primarily on cysteine residues, during the non-enzymatic reaction between reducing sugars and proteins (Abbas et al., 2016; Milanovic et al., 2022). This process, often termed glycoxidation, involves the generation of reactive oxygen species (ROS) and reactive carbonyl species (RCS) such as methylglyoxal, which lead to the depletion of the systemic thiol pool and the formation of advanced glycation end-products (AGEs) (Younus & Anwar, 2016; Ramful et al., 2018). Human serum albumin is a major target of this modification, as its single free thiol (Cys34) acts as a critical antioxidant that becomes impaired in hyperglycemic and oxidative stress states (Milanovic et al., 2022). The loss of free thiols is a significant biomarker for disease progression in conditions like diabetes mellitus and chronic kidney disease (Zhu et al., 2023; Dalle-Donne et al., 2006). Therapeutic strategies focus on protecting these thiol groups through the use of antioxidants, carbonyl scavengers, or thiol-donating compounds to maintain redox homeostasis and prevent tissue damage (Abbas et al., 2016; Younus & Anwar, 2016).

Other names

Protein thiol oxidationSulfhydryl oxidationGlycoxidation-induced thiol depletionProtein sulfhydryl loss

Antiglycation agents and antioxidants prevent thiol oxidation by scavenging reactive oxygen species (ROS) and reactive carbonyl species (RCS), thereby inhibiting the formation of advanced glycation end-products (AGEs) and preserving protein sulfhydryl groups (Abbas et al., 2016; Younus & Anwar, 2016).