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- Title
Inhibitory effects of mycosporine‐2‐glycine isolated from a halotolerant cyanobacterium on protein glycation and collagenase activity.
- Authors
Tarasuntisuk, S.; Patipong, T.; Hibino, T.; Waditee‐Sirisattha, R.; Kageyama, H.
- Abstract
Abstract: 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.
- Subjects
GLYCINE; COLLAGENASES; PROTEIN crosslinking; AMINO acids; AMINOGUANIDINE
- Publication
Letters in Applied Microbiology, 2018, Vol 67, Issue 3, p314
- ISSN
0266-8254
- Publication type
Article
- DOI
10.1111/lam.13041