Peptide name : Ascaphin-8

Source/Organism : Coastal Tailed Frog, Pacific Northwest, USA, North America

Linear/Cyclic : Not found

Chirality : L

Peptide length: 19

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 : Not found

Other activity : Anti-bacterial activity

Amino acid composition bar chart :

Molecular mass : 2019.4721 Dalton

Aliphatic index : 1.284

Instability index : -13.357

Hydrophobicity (GRAVY) : 0.7368

Isoelectric point : 10.001

Charge (pH 7) : 2.7572

Aromaticity : 0.105

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

Hydrophobic/hydrophilic ratio : 2.16666666

hydrophobic moment : -0.428

Missing amino acid : C,R,W,H,Q,P,M,I,E,S,Y,N

Most occurring amino acid : K

Most occurring amino acid frequency : 4

Least occurring amino acid : D

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.5, 0.1, 0.4)

SMILES Notation: CC(C)C[C@H](NC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1ccccc1)NC(=O)CN)C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1ccccc1)C(=O)O)C(C)C)[C@@H](C)O)C(C)C

1 : Conlon JM, et al. The ascaphins: a family of antimicrobial peptides from the skin secretions of the most primitive extant frog, Ascaphus truei. Biochem Biophys Res Commun. 2004; 320:170-5. doi: 10.1016/j.bbrc.2004.05.141

Paper title : The ascaphins: a family of antimicrobial peptides from the skin secretions of the most primitive extant frog, Ascaphus truei.

Doi : https://doi.org/10.1016/j.bbrc.2004.05.141

Abstract : The tailed frog Ascaphus truei occupies a unique position in phylogeny as the most primitive extant anuran and is regarded as the sister taxon to the clade of all other living frogs. Eight structurally related peptides, termed ascaphins 1-8, were isolated from norepinephrine-stimulated skin secretions of A. truei and were shown to possess differential growth inhibitory activity against Escherichia coli and Staphylococcus aureus. Ascaphins 2-7 may be represented by the consensus amino acid sequence GX2DX2KGAAKX3KTVAX2IANX.COOH whereas ascaphin-1 (GFRDVLKGAAKAFVKTVAGHIAN.NH2) and ascaphin-8 (GFKDLLKGAAKALVKTVLF.NH2) contain a C-terminally alpha-amidated residue. The ascaphins show no appreciable structural similarity with other families of antimicrobial peptides from frog skin but display limited sequence identity with the cationic, amphipathic alpha-helical peptides pandinin 1 and opistoporin 1, isolated from the venoms of African scorpions. Ascaphin-8 shows the highest potency against a range of pathogenic microorganisms but has the greatest haemolytic activity. The data indicate that the host defence strategy of using antimicrobial peptides in skin secretions arose early in the evolution of anurans.