Interaction of Zinc, Ascorbic Acid, and Folic Acid in Glycation with Albumin as Protein Model

Using albumin as model, we conducted series of in vitro glycation experiments to examine role of zinc in glycation using glucose at 4–100 mg/ml, incubations at 37°C or 60°C, duration of 2 or 4 weeks and in presence of zinc or ascorbic acid (AA) or folic acid (FA). Modifications of bovine serum albumin (BSA) were examined by using fluorescence of advanced glycation end products (AGEs) and dityrosine, UV, and Fourier transformed infrared spectroscopy. Adding zinc (0 to 768.5 μmol/l) resulted in significant inhibition of albumin glycation by glucose with a linear fit, $ y = - 0.0{895}x + {23}0.{99}left( {{R^2} = 0.{7676},p = 0.0{13}} right) $ . The glycation by fructose was greater than that of glucose with stronger inhibitory effect by zinc in fructose–glycation (t?=??5.8, p?=?0.002). Addition of zinc significantly decreased fluorescence as seen in Zn?+?FA or Zn?+?AA sets as compared to sets of FA alone (p?=?0.00056) or AA alone (p?=?0.037). The fluorescence for dityrosine and AGE had a correlation of 0.897 (p?