dbACP: A Comprehensive Database of Anti-Cancer Peptides

dbacp06391

General Description

Peptide name : Turgencin A

Source/Organism : Tunicate

Linear/Cyclic : Cyclic

Chirality : L

Sequence Information

Sequence : GPKTKAACKMACKLATCGKKPGGWKCKLCELGCDAV

Peptide length: 36

C-terminal modification: Cyclic

N-terminal modification : Amidation

Non-natural peptide information: None

Activity Information

Assay type : Human cell viability assay

Assay time : 72h

Activity : IC50 : 1.4 μM

Cell line : A2058

Cancer type : Melanoma cancer

Other activity : Anti-microbial activity

Physicochemical Properties

Amino acid composition bar chart :

Molecular mass : 3699.5464 Dalton

Aliphatic index : 0.544

Instability index : 49.6528

Hydrophobicity (GRAVY) : -0.116

Isoelectric point : 9.2445

Charge (pH 7) : 5.6966

Aromaticity : 0.027

Molar extinction coefficient (cysteine, cystine): (5500, 5875)

Hydrophobic/hydrophilic ratio : 2

hydrophobic moment : -0.285

Missing amino acid : R,H,Q,I,F,S,Y,N

Most occurring amino acid : K

Most occurring amino acid frequency : 8

Least occurring amino acid : M

Least occurring amino acid frequency : 1

Structural Information

3D structure :

Secondary structure fraction (Helix, Turn, Sheet): (0.5, 0.2, 0.1)

SMILES Notation: CSCC[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CS)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@@H]1CCCN1C(=O)CN)[C@@H](C)O)C(=O)N[C@@H](C)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)NCC(=O)NCC(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CS)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@H](C(=O)O)C(C)C)[C@@H](C)O

Secondary Structure :

Method Prediction
GOR CCCCHHHHHHHHHHHHTTCCCTCCTTTTTHTTCHHH
Chou-Fasman (CF) CCHHHHHHHHHHHHEECCCCCCCHHHHHHHCCCCCC
Neural Network (NN) CCCCHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCC
Joint/Consensus CCCCHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCC

Molecular Descriptors and ADMET Properties

Molecular Descriptors: Click here to download

ADMET Properties: Click here to download

Cross Referencing databases

Pubmed Id : 31940927

Uniprot : Click here

PDB : Not available

CancerPPD : Not available

ApIAPDB : Not available

CancerPPD2 ID : Not available

Reference

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

Literature

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<sub>Mox1</sub> 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<sub>50</sub> = 1.4 µM) and the human fibroblast cell line MRC-5 (IC<sub>50</sub> = 4.8 µM). The results from this study show that natural peptides isolated from marine tunicates have the potential to be promising drug leads.