Peptide name : [D-P L-P]cGm

Source/Organism : Synthetic construct

Linear/Cyclic : Cyclic

Chirality : L

Peptide length: 20

C-terminal modification: Cyclic

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : Cell viability assay

Assay time : 24h

Activity : CC50 : 51.5 ± 3.9 μM

Cell line : HeLa

Cancer type : Gastric cancer

Other activity : Anti-bacterial activity

Amino acid composition bar chart :

Molecular mass : 2415.8888 Dalton

Aliphatic index : 0.34

Instability index : 43.56

Hydrophobicity (GRAVY) : -0.96

Isoelectric point : 9.931

Charge (pH 7) : 5.7175

Aromaticity : 0.1

Molar extinction coefficient (cysteine, cystine): (2980, 3230)

Hydrophobic/hydrophilic ratio : 0.9

hydrophobic moment : 0.3983

Missing amino acid : W,H,M,I,E,F,S,D,N,A

Most occurring amino acid : R

Most occurring amino acid frequency : 5

Least occurring amino acid : L

Least occurring amino acid frequency : 1

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

SMILES Notation: CC(C)C[C@H](NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CS)NC(=O)CN)C(=O)N[C@@H](CS)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(=N)N)C(=O)NCC(=O)N1CCC[C@H]1C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCNC(=N)N)C(=O)O)[C@@H](C)O)C(C)C

1 : Troeira Henriques S, et al. Redesigned Spider Peptide with Improved Antimicrobial and Anticancer Properties. ACS Chem Biol. 2017; 12:2324-2334. doi: 10.1021/acschembio.7b00459

Paper title : Redesigned Spider Peptide with Improved Antimicrobial and Anticancer Properties.

Doi : https://doi.org/10.1021/acschembio.7b00459

Abstract : Gomesin, a disulfide-rich antimicrobial peptide produced by the Brazilian spider Acanthoscurria gomesiana, has been shown to be potent against Gram-negative bacteria and to possess selective anticancer properties against melanoma cells. In a recent study, a backbone cyclized analogue of gomesin was shown to be as active but more stable than its native form. In the current study, we were interested in improving the antimicrobial properties of the cyclic gomesin, understanding its selectivity toward melanoma cells and elucidating its antimicrobial and anticancer mode of action. Rationally designed analogues of cyclic gomesin were examined for their antimicrobial potency, selectivity toward cancer cells, membrane-binding affinity, and ability to disrupt cell and model membranes. We improved the activity of cyclic gomesin by ∼10-fold against tested Gram-negative and Gram-positive bacteria without increasing toxicity to human red blood cells. In addition, we showed that gomesin and its analogues are more toxic toward melanoma and leukemia cells than toward red blood cells and act by selectively targeting and disrupting cancer cell membranes. Preference toward some cancer types is likely dependent on their different cell membrane properties. Our findings highlight the potential of peptides as antimicrobial and anticancer leads and the importance of selectively targeting cancer cell membranes for drug development.