Peptide name : Brevinin-1DYb

Source/Organism : Dybowski's frog, or Siberian wood frog, Asia

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 20

C-terminal modification: Not found

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Not found

Cancer type : Not found

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 2239.8688 Dalton

Aliphatic index : 1.515

Instability index : 17

Hydrophobicity (GRAVY) : 1.6

Isoelectric point : 9.3902

Charge (pH 7) : 2.7373

Aromaticity : 0.15

Molar extinction coefficient (cysteine, cystine): (0, 125)

Hydrophobic/hydrophilic ratio : 4

hydrophobic moment : 0.2381

Missing amino acid : R,W,H,Q,T,M,E,D,Y,N,V,G

Most occurring amino acid : L

Most occurring amino acid frequency : 6

Least occurring amino acid : S

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.6, 0.1, 0.5)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)Cc1ccccc1)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)O

1 : Conlon JM, et al. Cytolytic peptides belonging to the brevinin-1 and brevinin-2 families isolated from the skin of the Japanese brown frog, Rana dybowskii. Toxicon. 2007; 50:746-56. doi: 10.1016/j.toxicon.2007.06.023

Paper title : Cytolytic peptides belonging to the brevinin-1 and brevinin-2 families isolated from the skin of the Japanese brown frog, Rana dybowskii.

Doi : https://doi.org/10.1016/j.toxicon.2007.06.023

Abstract : Peptidomic analysis of an extract of the skins of specimens of Dybowski's brown frog Rana dybowskii Gunther, 1876, collected on Tsushima Island, Japan led to the identification of 10 peptides with differential antibacterial and hemolytic activities. The primary structures of these peptides identified them as belonging to the brevinin-1 (5 peptides) and brevinin-2 (5 peptides) families of antimicrobial peptides. A peptide (FIGPIISALASLFG.NH(2)) with structural similarity to members of the temporin family was also isolated but this component lacked cytolytic activity. Phylogenetic relationships among the Japanese brown frogs (R. dybowskii, R. japonica, R. okinavana, R. ornativentris, R. pirica, R. sakuraii, R. tagoi, and R. tsushimensis) are only incompletely understood. Cladograms based upon maximum parsimony analyses of the brevinin-1 and brevinin-2 amino acid sequences provide strong support for a sister-group relationship between R. dybowskii and R. pirica and somewhat weaker support for a sister-group relationship between R. okinavana and R. tsushimensis. These conclusions are consistent with previous analyses based upon allozyme variations and comparisons of the nucleotide sequences of mitochondrial genes.