Exploring the impact of reducing agent on glycated protein aggregation: Insights from insulin and lysozyme

Elevated blood glucose levels lead to non-enzymatic glycation, a process that is particularly troublesome for those with diabetes. With the projected increase in diabetes cases globally, it is important to investigate the impact of physiological processes such as reduction or oxidation on the stability and aggregation of glycated proteins. This study investigates the impact of dithiothreitol (DTT), a reducing agent, on the stability of glycated and non-glycated proteins using insulin and lysozyme as model proteins. Various biophysical techniques were utilized to examine glycation, conformational changes, and aggregation of insulin and lysozyme in the presence of DTT. This study showed that DTT can disrupt the delicate balance of disulfide bonds in native proteins, and the robust structure imparted by advanced glycation end-products (AGEs) in glycated proteins renders them more resistant to the denaturing effects of DTT. This has wide-ranging ramifications in fields such as biotechnology and neurological disease research.