Peptide name : Gomesin

Source/Organism : Tarantula spider sp.

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 18

C-terminal modification: Not found

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : Lactate dehydrogenase (LDH) assay

Assay time : 24h

Activity : MIC : 10 mM

Cell line : U-87 MG

Cancer type : Glioblastoma

Other activity : Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 2221.6584 Dalton

Aliphatic index : 0.377

Instability index : 40.7778

Hydrophobicity (GRAVY) : -0.888

Isoelectric point : 9.931

Charge (pH 7) : 5.7175

Aromaticity : 0.111

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

Hydrophobic/hydrophilic ratio : 0.8

hydrophobic moment : 0.5315

Missing amino acid : W,H,P,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, 0.1, 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)N[C@@H](CCCNC(=N)N)C(=O)O)[C@@H](C)O)C(C)C

1 : Barbosa FM, et al. Gomesin, a peptide produced by the spider Acanthoscurria gomesiana, is a potent anticryptococcal agent that acts in synergism with fluconazole. FEMS Microbiol Lett. 2007; 274:279-86. doi: 10.1111/j.1574-6968.2007.00850.x

Paper title : Gomesin, a peptide produced by the spider Acanthoscurria gomesiana, is a potent anticryptococcal agent that acts in synergism with fluconazole.

Doi : https://doi.org/10.1111/j.1574-6968.2007.00850.x

Abstract : Gomesin is an 18-residue cysteine-rich antimicrobial peptide produced by hemocytes of the spider Acanthoscurria gomesiana. In the present study, the antifungal properties of gomesin against Cryptococcus neoformans, the etiologic agent of cryptococcosis, were evaluated. Gomesin bound to the cell surface of cryptococci, which resulted in cell death associated with membrane permeabilization. Antifungal concentrations of gomesin were not toxic for human brain cells. Supplementation of cryptococcal cultures with the peptide (1 microM) caused a decrease in capsule expression and rendered fungal cells more susceptible to killing by human brain phagocytes. The possible use of gomesin in combination with fluconazole, a standard antifungal drug, was also evaluated. In association with fluconazole, gomesin concentrations with low antimicrobial activity (0.1-1 microM) inhibited fungal growth and enhanced the antimicrobial activity of brain phagocytes. These results reveal the potential of gomesin to promote inhibition of cryptococcal growth directly or by enhancing the effectiveness of host defenses.