Dataset related to the article "N-Acetylcysteine, N-Acetylcysteine Amide, and Thioredoxin Mimetic Peptides Regenerate Mercaptoalbumin and Exhibit Antioxidant Activity"

This record contains row data related to the article "N-Acetylcysteine, N-Acetylcysteine Amide, and Thioredoxin  Mimetic Peptides Regenerate Mercaptoalbumin and Exhibit Antioxidant Activity"

Abstract:[M1] [ES2]  Albumin (HSA) is the most abundant circulating protein and plays a pivotal role in maintaining the redox state of the plasma. Three HSA proteoforms have been identified based on the redox state of cysteine 34. These include the reduced proteoform (HSA-SH), non-mercaptoalbumin-1, containing a disulfide with small thiols such as cysteine (HSA-Cys), and non-mercaptoalbumin-2, the higher oxidized proteoform. Several clinical studies have shown a relationship between an individual’s serum HSA redox status and the severity of diseases such as heart failure, diabetes mellitus, and liver disease. Furthermore, when HSA undergoes oxidation, it can worsen certain health conditions and contribute to their advancement. This study aimed to evaluate the ability of the redox compounds AD4/NACA and the thioredoxin mimetic (TXM) peptides TXM-CB3, TXM-CB13, and TXM-CB30 to regenerate HSA-SH and to improve its redox activity. The HSA proteoforms were quantified by LC-MS, and the antioxidant activity was determined using dichlorofluorescin. Each of the compounds exhibited a significant increase in HSA-SH and a reduction in HSA-Cys levels. The increase in HSA-SH was associated with a recovery of its antioxidant activity. Herein, we reveal a new mechanistic facet contributing to the antioxidant activity of AD4/NACA and TXM peptides. These antioxidant properties propose an additional therapeutic approach for addressing oxidative stress-related conditions.