Abstract

Protein glycation with sugars such as glucose start by the initial reaction between the carbonyl group of sugars and the amino group of proteins such as albumin and hemoglobin. This leads to the generation of Schiff base and following that the amadori and advanced glycation end products (AGEs). AGEs products can store in tissues and blood of diabetic patients. So, they play key roles to generate free radicals, which cause the development of diabetes complications. Inhibition of protein glycation plays an important role in controlling diabetes, so the identification of anti-glycation compounds is now receiving considerable interest. In this study, the protection effects of thymoquinone and its mixture with p-cymene on the glycation of bovine serum albumin (BSA) have been investigated by differential pulse voltammetry (DPV) and UV–vis spectrophotometry (UV–vis) techniques. Also, the multivariate curve resolution–alternating least squares (MCR–ALS) method was used since the results of the experimental measurements have a strongly overlapping signals. Molecular docking was applied to determine the site specific binding of inhibitor with residues of BSA. This study demonstrates that thymoquinone and its mixture with p-cymene have the potent ability to use as a dietary adjuvant against glycation.

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