Phlorotannins Remarkably Suppress the Formation of Nε-(Carboxymethyl)lysine in a Collagen-Glyoxal Environment

N ε-(Carboxymethyl)lysine (CML), which is formed by the glycation of collagen, is a skin-accumulating advanced glycation end product and has been shown to be deeply involved in diabetic osteopenia and skin aging. In this study, we prepared the phlorotannins of marine algal polyphenols from Japanese Lessoniaceae ( Ecklonia cava, Ecklonia kurome, cultured E. kurome, Ecklonia stolonifera, Eisenia nipponica, and Eisenia bicyclis) and evaluated their inhibitory activities against CML formation in a collagen-glyoxal environment. The level of CML formed from the glycation of collagen by glyoxal was detected using an enzyme-linked immunosorbent assay. Except for E. stolonifera, the level of CML formation in the treatment with crude phlorotannins at 0.16 µg/mL was found to be comparable to that in the treatment with 0.40 mM aminoguanidine hydrochloride (AG) which is a typical antiglycation agent. In the test using phloroglucinol and isolated eckols (eckol, fucofuroeckol A, phlorofucofuroeckol A, dieckol, and 8,8’-bieckol) at a concentration of 0.80 µg/mL, the level of CML formed was lower for each compound, except for phlorofucofuroeckol A, than the data obtained with the addition of 2.0 mM AG. The mass concentration of 0.80 µg/mL was converted to 6.3 µM for phloroglucinol, 2.2 µM for eckol, 1.7 µM for fucofuroeckol A, 1.3 µM for phlorofucofuroeckol A, and 1.1 µM for dieckol and 8,8’-bieckol. From a comparison of the molar concentrations, it was found that phloroglucinol and the eckols inhibited the formation of CML resulting from glycation of collagen by glyoxal at concentrations of approximately 317 to 1818 times lower than AG.