Magnificamide, a β-defensin-like peptide from the mucus of the sea anemone Heteractis magnifica, is a strong inhibitor of mammalian α-amylases
Sintsova, O.; Kalinovskii, A.; Gladkikh, I.; Zelepuga, E.; Monastyrnaya, M.; Kim, N.; Shevchenko, L.; Peigneur, S.; Tytgat, J.; Kozlovskaya, E.; Leychenko, E. (2019). Magnificamide, a β-defensin-like peptide from the mucus of the sea anemone Heteractis magnifica, is a strong inhibitor of mammalian α-amylases. Mar. Drugs 17(10): 542. https://dx.doi.org/10.3390/md17100542 In: Marine Drugs. Molecular Diversity Preservation International (MDPI): Basel. ISSN 1660-3397; e-ISSN 1660-3397, more |   |
| Keywords | Cnidaria [WoRMS]
Marine/Coastal | | Author keywords | Cnidaria; sea anemones; venom; amylase inhibitors; defensin; diabetes |
| Authors | | Top | - Sintsova, O.
- Kalinovskii, A.
- Gladkikh, I.
- Zelepuga, E.
| - Monastyrnaya, M.
- Kim, N.
- Shevchenko, L.
- Peigneur, S., more
| - Tytgat, J., more
- Kozlovskaya, E.
- Leychenko, E.
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| Abstract | Sea anemones’ venom is rich in peptides acting on different biological targets, mainly on cytoplasmic membranes and ion channels. These animals are also a source of pancreatic α-amylase inhibitors, which have the ability to control the glucose level in the blood and can be used for the treatment of prediabetes and type 2 diabetes mellitus. Recently we have isolated and characterized magnificamide (44 aa, 4770 Da), the major α-amylase inhibitor of the sea anemone Heteractis magnifica mucus, which shares 84% sequence identity with helianthamide from Stichodactyla helianthus. Herein, we report some features in the action of a recombinant analog of magnificamide. The recombinant peptide inhibits porcine pancreatic and human saliva α-amylases with Ki’s equal to 0.17 ± 0.06 nM and 7.7 ± 1.5 nM, respectively, and does not show antimicrobial or channel modulating activities. We have concluded that the main function of magnificamide is the inhibition of α-amylases; therefore, its functionally active recombinant analog is a promising agent for further studies as a potential drug candidate for the treatment of the type 2 diabetes mellitus. |
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