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Article

New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties

by
Yulia A. Logashina
1,2,†,
Runar Gjerp Solstad
3,†,
Konstantin S. Mineev
1,4,
Yuliya V. Korolkova
1,
Irina V. Mosharova
1,
Igor A. Dyachenko
5,6,
Victor A. Palikov
5,6,
Yulia A. Palikova
5,6,
Arkadii N. Murashev
5,
Alexander S. Arseniev
1,
Sergey A. Kozlov
1,
Klara Stensvåg
3,
Tor Haug
3,* and
Yaroslav A. Andreev
1,2,*
1
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, Russia
2
Sechenov First Moscow State Medical University, Institute of Molecular Medicine,Trubetskaya str. 8, bld. 2, Moscow 119991, Russia
3
Faculty of Biosciences, Fisheries and Economics, Norwegian College of Fishery Science, UiT—The Arctic University of Norway, NO 9037 Tromsø, Norway
4
Moscow Institute of Physics and Technology, Institutskyi per., 9, Dolgoprudnyi, 141700, Moscow, Russia
5
Branch of the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 6 Nauki Avenue, 142290 Pushchino, Russia
6
Pushchino State Natural-Science Institute, 142290 Pushchino, Russia
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Toxins 2017, 9(5), 154; https://doi.org/10.3390/toxins9050154
Submission received: 16 February 2017 / Revised: 27 April 2017 / Accepted: 27 April 2017 / Published: 29 April 2017
(This article belongs to the Section Marine and Freshwater Toxins)

Abstract

A novel bioactive peptide named τ-AnmTx Ueq 12-1 (short name Ueq 12-1) was isolated and characterized from the sea anemone Urticina eques. Ueq 12-1 is unique among the variety of known sea anemone peptides in terms of its primary and spatial structure. It consists of 45 amino acids including 10 cysteine residues with an unusual distribution and represents a new group of sea anemone peptides. The 3D structure of Ueq 12-1, determined by NMR spectroscopy, represents a new disulfide-stabilized fold partly similar to the defensin-like fold. Ueq 12-1 showed the dual activity of both a moderate antibacterial activity against Gram-positive bacteria and a potentiating activity on the transient receptor potential ankyrin 1 (TRPA1). Ueq 12-1 is a unique peptide potentiator of the TRPA1 receptor that produces analgesic and anti-inflammatory effects in vivo. The antinociceptive properties allow us to consider Ueq 12-1 as a potential analgesic drug lead with antibacterial properties.
Keywords: sea anemones; innate immunity; defensive strategies; TRPA1 receptor; antimicrobial sea anemones; innate immunity; defensive strategies; TRPA1 receptor; antimicrobial
Graphical Abstract

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MDPI and ACS Style

Logashina, Y.A.; Solstad, R.G.; Mineev, K.S.; Korolkova, Y.V.; Mosharova, I.V.; Dyachenko, I.A.; Palikov, V.A.; Palikova, Y.A.; Murashev, A.N.; Arseniev, A.S.; et al. New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties. Toxins 2017, 9, 154. https://doi.org/10.3390/toxins9050154

AMA Style

Logashina YA, Solstad RG, Mineev KS, Korolkova YV, Mosharova IV, Dyachenko IA, Palikov VA, Palikova YA, Murashev AN, Arseniev AS, et al. New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties. Toxins. 2017; 9(5):154. https://doi.org/10.3390/toxins9050154

Chicago/Turabian Style

Logashina, Yulia A., Runar Gjerp Solstad, Konstantin S. Mineev, Yuliya V. Korolkova, Irina V. Mosharova, Igor A. Dyachenko, Victor A. Palikov, Yulia A. Palikova, Arkadii N. Murashev, Alexander S. Arseniev, and et al. 2017. "New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties" Toxins 9, no. 5: 154. https://doi.org/10.3390/toxins9050154

APA Style

Logashina, Y. A., Solstad, R. G., Mineev, K. S., Korolkova, Y. V., Mosharova, I. V., Dyachenko, I. A., Palikov, V. A., Palikova, Y. A., Murashev, A. N., Arseniev, A. S., Kozlov, S. A., Stensvåg, K., Haug, T., & Andreev, Y. A. (2017). New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties. Toxins, 9(5), 154. https://doi.org/10.3390/toxins9050154

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