New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties
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 cyst...
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| Format: | Article |
| Language: | English |
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MDPI AG
2017-04-01
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| Series: | Toxins |
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| Online Access: | http://www.mdpi.com/2072-6651/9/5/154 |
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| author | Yulia A. Logashina 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 Sergey A. Kozlov Klara Stensvåg Tor Haug Yaroslav A. Andreev |
| author_facet | Yulia A. Logashina 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 Sergey A. Kozlov Klara Stensvåg Tor Haug Yaroslav A. Andreev |
| author_sort | Yulia A. Logashina |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-11T22:51:44Z |
| format | Article |
| id | doaj.art-5dadd07db16d43ca934dcd5b2be561da |
| institution | Directory Open Access Journal |
| issn | 2072-6651 |
| language | English |
| last_indexed | 2024-04-11T22:51:44Z |
| publishDate | 2017-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Toxins |
| spelling | doaj.art-5dadd07db16d43ca934dcd5b2be561da2022-12-22T03:58:33ZengMDPI AGToxins2072-66512017-04-019515410.3390/toxins9050154toxins9050154New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating PropertiesYulia A. Logashina0Runar Gjerp Solstad1Konstantin S. Mineev2Yuliya V. Korolkova3Irina V. Mosharova4Igor A. Dyachenko5Victor A. Palikov6Yulia A. Palikova7Arkadii N. Murashev8Alexander S. Arseniev9Sergey A. Kozlov10Klara Stensvåg11Tor Haug12Yaroslav A. Andreev13Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, RussiaFaculty of Biosciences, Fisheries and Economics, Norwegian College of Fishery Science, UiT—The Arctic University of Norway, NO 9037 Tromsø, NorwayShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, RussiaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, RussiaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, RussiaBranch of the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 6 Nauki Avenue, 142290 Pushchino, RussiaBranch of the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 6 Nauki Avenue, 142290 Pushchino, RussiaBranch of the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 6 Nauki Avenue, 142290 Pushchino, RussiaBranch of the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 6 Nauki Avenue, 142290 Pushchino, RussiaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, RussiaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, RussiaFaculty of Biosciences, Fisheries and Economics, Norwegian College of Fishery Science, UiT—The Arctic University of Norway, NO 9037 Tromsø, NorwayFaculty of Biosciences, Fisheries and Economics, Norwegian College of Fishery Science, UiT—The Arctic University of Norway, NO 9037 Tromsø, NorwayShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, RussiaA 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.http://www.mdpi.com/2072-6651/9/5/154sea anemonesinnate immunitydefensive strategiesTRPA1 receptorantimicrobial |
| spellingShingle | Yulia A. Logashina 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 Sergey A. Kozlov Klara Stensvåg Tor Haug Yaroslav A. Andreev New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties Toxins sea anemones innate immunity defensive strategies TRPA1 receptor antimicrobial |
| title | New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties |
| title_full | New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties |
| title_fullStr | New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties |
| title_full_unstemmed | New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties |
| title_short | New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties |
| title_sort | new disulfide stabilized fold provides sea anemone peptide to exhibit both antimicrobial and trpa1 potentiating properties |
| topic | sea anemones innate immunity defensive strategies TRPA1 receptor antimicrobial |
| url | http://www.mdpi.com/2072-6651/9/5/154 |
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