Abstract
•Glycated albumin is more prone to SDS-induced aggregation than non-glycated albumin.•Glycated albumin solubilized at lower SDS concentration than non-glycated albumin.•Glycated albumin lost secondary structure at lower SDS concentration.
Diabetes prevails worldwide in all age groups, and the number is expected to increase to 366 million in 2030. The non-enzymatic glycation enhanced many folds in diabetic conditions. Moreover, non-enzymatic glycation worsens the disease complications and makes health management difficult. In earlier studies, anionic surfactants were found to induce aggregation and amyloid formation by interacting with the protonated basic residues of the proteins. Interestingly, basic residues are also primary glycation sites. Therefore, the number of unmodified Lys and Arg residues in the glycated proteins will be lesser than in the non-glycated protein. Consequently, a lower amount of anionic surfactants is required to neutralize the glycated proteins charges and thus for aggregation and amyloid formation. Therefore, the mechanism of anionic surfactant-induced aggregation and amyloid formation of glycated protein should be different. Our results showed that glycated BSA tends to aggregate at 10-fold lower SDS concentrations than non-glycated BSA. Interestingly, the aggregates of glycated BSA also solubilize similar to non-glycated BSA. Due to the reduced threshold of anionic surfactant-induced aggregation in the glycated proteins, they become more prone to aggregation.