Serum albumin is the most abundant plasma protein with a large number of lysine and arginine residues. Hence, it is highly susceptible to glycation, a non-enzymatic reaction involving binding of non-reducing sugars to proteins, in vivo. Oxidative stress is known to promote glycation and the Advanced glycation end products (AGEs) formed through glycation bind to their cell-surface receptor (RAGE). AGE-RAGE interaction activates downstream intracellular signaling pathways resulting in increased inflammation and oxidative stress and the vicious cycle of Oxidative stress and AGE formation continues. Here we quantified glycated albumin peptides mass spectrometrically in maternally separated rats and compared their levels with those in Control to investigte if AGE accumulation is associated with the increased inflammation and oxidative stress in MS rats.