期刊
TOXINS
卷 9, 期 5, 页码 -出版社
MDPI AG
DOI: 10.3390/toxins9050154
关键词
sea anemones; innate immunity; defensive strategies; TRPA1 receptor; antimicrobial
资金
- programme of Presidium of RAS Molecular and Cell Biology
- President of RF [SSh-7676.2016.4]
- Functional Genomics (FUGE) programme
- Biotek programme of the Research Council of Norway, project XBioPepS [208546]
- Russian Science Foundation [16-15-00167]
- Russian Science Foundation [16-15-00167] Funding Source: Russian Science Foundation
A novel bioactive peptide named tau-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.
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