Organosulfur mimics of S-allyl cysteine and effects on advanced glycation end-products

Diabetes mellitus (DM) is a metabolic disorder characterised by increased blood glucose concentrations resulting from a deficiency of insulin, or insulin resistance. The prolonged hyperglycaemia of DM is extensively recognised as the causal link between diabetes and diabetic complications. Moreover, hyperglycaemia induces protein glycation and the formation of advanced glycation endproducts (AGEs). The accumulation of AGE in the body leads to structural and functional modifications of tissue proteins. Herein we evaluate the anti-glycation activities of several inhibitors i.e. S-allyl cysteine (SAC), Nacetylcysteine (NAC) and synthesised small molecule inhibitors that mimic SAC/NAC (compounds A, B and C) identified as inhibiting the formation of methylglyoxal (MG)-derived AGE. The extent of glycation in the presence and absence of SAC, NAC and compound A were assessed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). It has been established that SAC, NAC and compound A, are inhibitors of protein glycation.