Peptide name : Turgencin B

Source/Organism : Tunicate

Linear/Cyclic : Cyclic

Chirality : L

Peptide length: Not available

C-terminal modification: Cyclic

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : Human cell viability assay

Assay time : 72h

Activity : IC50 : 4.1μM

Cell line : A2058

Cancer type : Melanoma cancer

Other activity : Anti-microbial activity

Amino Acid Composition Bar Chart : Not available

Molecular mass : Not available

Aliphatic index : Not available

Instability index : Not available

Hydrophobicity (GRAVY) : Not available

Isoelectric point : Not available

Charge (pH 7) : Not available

Aromaticity : Not available

Molar extinction coefficient (cysteine, cystine): Not available

Hydrophobic/hydrophilic ratio : Not available

hydrophobic moment : Not available

Missing amino acid : Not available

Most occurring amino acid : Not available

Most occurring amino acid frequency : Not available

Least occurring amino acid : Not available

Least occurring amino acid frequency : Not available

3D-structure: Not available

Secondary structure fraction (Helix, Turn, Sheet): Not available

SMILES Notation: Not available

Molecular descriptors: Not available

ADMET properties: Not available

1 : Hansen IKØ, et al. Isolation and Characterization of Antimicrobial Peptides with Unusual Disulfide Connectivity from the Colonial Ascidian Synoicum turgens. Mar Drugs. 2020; 18:(unknown pages). doi: 10.3390/md18010051

Paper title : Isolation and Characterization of Antimicrobial Peptides with Unusual Disulfide Connectivity from the Colonial Ascidian Synoicum turgens.

Doi : https://doi.org/10.3390/md18010051

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 Cys1-Cys6, Cys2-Cys5, and Cys3-Cys4 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_Mox1 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 (IC₅₀ = 1.4 µM) and the human fibroblast cell line MRC-5 (IC₅₀ = 4.8 µM). The results from this study show that natural peptides isolated from marine tunicates have the potential to be promising drug leads.