Abstract
Recently, the important role of the Maillard reaction in the development of diabetic complications has been attracting attention. The Maillard reaction is a non-enzymatic reaction between aldehyde groups of reducing sugars and free side chains on amino acids, especially lysine residues of proteins. We investigated the possible inhibition of the Maillard reaction by 1-lysine, which is one of the essential amino acids and is usually taken in through foods.
L-lysine increased the total fluorescence intensity of the incubation mixture, but slightly decreased the furosine level generated on BSA. L-lysine inhibited the glucose-induced polymerization of lysozyme and acted on 3-deoxyglucosone (3DG), an active cross-linker of the Maillard reaction, to inhibit the 3DG-induced polymerization.
Exogenously applied 1-lysine was considered to compete with lysine residues of protein for glucose and trapped active carbonyl intermediates. Thus, these results suggest that 1-lysine inhibits the Maillard reaction.
