Back to Search
Start Over
Isolation and Characterization of Antimicrobial Peptides with Unusual Disulfide Connectivity from the Colonial Ascidian Synoicum turgens.
- Source :
- Marine Drugs; Jan2020, Vol. 18 Issue 1, p51-51, 1p
- Publication Year :
- 2020
-
Abstract
- This study reports the isolation of two novel cysteine-rich antibacterial peptides, turgencin A and turgencin B, along with their oxidized derivatives, from the Arctic marine colonial ascidian Synoicum turgens. The peptides are post-translationally modified, containing six cysteines with an unusual disulfide connectivity of Cys<superscript>1</superscript>-Cys<superscript>6</superscript>, Cys<superscript>2</superscript>-Cys<superscript>5</superscript>, and Cys<superscript>3</superscript>-Cys<superscript>4</superscript> and an amidated C-terminus. Furthermore, the peptides contain methionine residues resulting in the isolation of peptides with different degrees of oxidation. The most potent peptide, turgencin A<subscript>Mox1</subscript> with one oxidized methionine, displayed antimicrobial activity against both Gram-negative and Gram-positive bacteria with a minimum inhibitory concentration (MIC) as low as 0.4 µM against selected bacterial strains. In addition, the peptide inhibited the growth of the melanoma cancer cell line A2058 (IC<subscript>50</subscript> = 1.4 µM) and the human fibroblast cell line MRC-5 (IC<subscript>50</subscript> = 4.8 µM). The results from this study show that natural peptides isolated from marine tunicates have the potential to be promising drug leads. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 16603397
- Volume :
- 18
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- Marine Drugs
- Publication Type :
- Academic Journal
- Accession number :
- 141410869
- Full Text :
- https://doi.org/10.3390/md18010051