Mycosporine-2-glycine (M2G), isolated from the halotolerant cyanobacterium Aphanothece halophytica, was purified and characterized in order to determine its utility as a cosmetic and pharmaceutical ingredient. M2G efficiently inhibited protein crosslinking. The inhibitory activity of M2G was significantly greater than that of the well-known Maillard reaction inhibitor aminoguanidine. In addition, M2G and other known mycosporine-like amino acids inhibited bacterial collagenase activity. To the best of our knowledge, this is the first report describing that M2G specifically inhibits the formation of advanced glycation end-products (AGEs), which play a critical role in ageing process and age-related diseases. These observations indicate that M2G may have potential therapeutic applications by suppressing the formation of AGEs and inhibiting excess collagenase activity.
Significance and impact of the study: Mycosporine-like amino acids (MAAs) are known as multifunctional natural compounds. The MAA mycosporine-2-glycine (M2G), isolated from the halotolerant cyanobacterium Aphanothece halophytica, has potential therapeutic applications for the prevention of skin ageing. Purified M2G was endotoxin-free. M2G had greater inhibitory activity of protein cross-linking compared with well-known inhibitor, aminoguanidine and hindered bacterial collagenase activity. The mechanisms for these inhibitory activities of M2G are discussed in this study.
Keywords: collagenase; metal chelating; mycosporine-2-glycine; mycosporine-like amino acid; protein cross-linking.
© 2018 The Society for Applied Microbiology.