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.

doi:/10.3390/md17100542

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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

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VLIZ: Open access 343608 [ download pdf ]

Trefwoorden

Cnidaria [WoRMS]
Marien/Kust

Author keywords

Cnidaria; sea anemones; venom; amylase inhibitors; defensin; diabetes

Auteurs		Top
Sintsova, O. Kalinovskii, A. Gladkikh, I. Zelepuga, E.	Monastyrnaya, M. Kim, N. Shevchenko, L. Peigneur, S., meer	Tytgat, J., meer Kozlovskaya, E. Leychenko, E.

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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