Peptide name : Gomesin

Source/Organism : Hemocytes, Tarantula spider sp.

Linear/Cyclic : Not found

Chirality : L

Peptide length: 18

C-terminal modification: Not found

N-terminal modification : Free

Non-natural peptide information: None

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Not found

Cancer type : Breast cancer

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 2292.7363 Dalton

Aliphatic index : 0.377

Instability index : 36.5889

Hydrophobicity (GRAVY) : -1.061

Isoelectric point : 9.931

Charge (pH 7) : 5.7175

Aromaticity : 0.111

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

Hydrophobic/hydrophilic ratio : 0.63636363

hydrophobic moment : 0.3593

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, 0.0, 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)[C@@H](N)CCC(N)=O)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 : Silva PI, et al. Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family. J Biol Chem. 2000; 275:33464-70. doi: 10.1074/jbc.M001491200

Paper title : Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family.

Doi : https://doi.org/10.1074/jbc.M001491200

Abstract : We have purified a small size antimicrobial peptide, named gomesin, from the hemocytes of the unchallenged tarantula spider Acanthoscurria gomesiana. Gomesin has a molecular mass of 2270.4 Da, with 18 amino acids, including a pyroglutamic acid as the N terminus, a C-terminal arginine alpha-amide, and four cysteine residues forming two disulfide bridges. This peptide shows marked sequence similarities to antimicrobial peptides from other arthropods such as tachyplesin and polyphemusin from horseshoe crabs and androctonin from scorpions. Interestingly, it also shows sequence similarities to protegrins, antimicrobial peptides from porcine leukocytes. Gomesin strongly affects bacterial growth, as well as the development of filamentous fungi and yeast. In addition, we showed that gomesin affects the viability of the parasite Leishmania amazonensis.