Next Article in Journal
Distinct Expression of Immunoglobulin-Binding Proteins in Shiga Toxin-Producing Escherichia coli Implicates High Protein Stability and a Characteristic Phenotype
Previous Article in Journal
Development of an Immunochromatographic Strip Test for the Rapid Detection of Alternariol Monomethyl Ether in Fruit
Article Menu
Issue 5 (May) cover image

Export Article

Open AccessArticle
Toxins 2017, 9(5), 154; doi:10.3390/toxins9050154

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

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
These authors contributed equally to this work.
*
Authors to whom correspondence should be addressed.
Academic Editor: Richard J. Lewis
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)
View Full-Text   |   Download PDF [6253 KB, uploaded 4 May 2017]   |  

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. View Full-Text
Keywords: sea anemones; innate immunity; defensive strategies; TRPA1 receptor; antimicrobial sea anemones; innate immunity; defensive strategies; TRPA1 receptor; antimicrobial
Figures

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

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.; Kozlov, S.A.; Stensvåg, K.; Haug, T.; Andreev, Y.A. New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties. Toxins 2017, 9, 154.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Toxins EISSN 2072-6651 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top