Diabetes Mellitus (DM) is a metabolic disorder characterised by increased blood glucose concentrations resulting from a lack or partial 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 end-products (AGEs). The accumulation of AGEs in the body leads to structural and functional modifications of tissue proteins. The present study was conducted to evaluate the antiglycation activities of several inhibitors i.e. S-allyl cysteine (SAC), N-acetylcysteine (NAC) and compounds A, B and C (chemically synthesised small molecule inhibitors that mimic SAC/NAC) were identified as inhibiting the formation of Methylglyoxal (MG)-derived AGEs. 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.