Peptide name : Aurein-3.2

Source/Organism : Southern bell frog

Linear/Cyclic : Linear

Chirality : L

Peptide length: 17

C-terminal modification: Linear

N-terminal modification : Free

Non-natural peptide information: None

Assay type : One-dose and five-dose assay

Assay time : 24h

Activity : IC50 : 5 μM

Cell line : Not found

Cancer type : Prostate cancer

Other activity : Antibiotic activity

Amino acid composition bar chart :

Molecular mass : 1769.0924 Dalton

Aliphatic index : 1.435

Instability index : 42.1647

Hydrophobicity (GRAVY) : 0.9118

Isoelectric point : 8.5984

Charge (pH 7) : 0.8464

Aromaticity : 0.058

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

Hydrophobic/hydrophilic ratio : 1.83333333

hydrophobic moment : -1.170

Missing amino acid : C,R,W,Q,T,P,M,E,Y,N

Most occurring amino acid : I

Most occurring amino acid frequency : 4

Least occurring amino acid : L

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.2, 0.4)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(C)C)NC(=O)CN)[C@@H](C)CC)C(C)C)[C@@H](C)CC)[C@@H](C)CC)C(=O)O

1 : Rozek T, et al. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2. Eur J Biochem. 2000; 267:5330-41. doi: 10.1046/j.1432-1327.2000.01536.x

Paper title : The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2.

Doi : https://doi.org/10.1046/j.1432-1327.2000.01536.x

Abstract : Seventeen aurein peptides are present in the secretion from the granular dorsal glands of the Green and Golden Bell Frog Litoria aurea, and 16 from the corresponding secretion of the related Southern Bell Frog L. raniformis. Ten of these peptides are common to both species. Thirteen of the aurein peptides show wide-spectrum antibiotic and anticancer activity. These peptides are named in three groups (aureins 1-3) according to their sequences. Amongst the more active peptides are aurein 1.2 (GLFDIIKKIAESF-NH2), aurein 2.2 (GLFDIVKKVVGALGSL-NH2) and aurein 3.1 (GLFDIVKKIAGHIAGSI-NH2). Both L. aurea and L. raniformis have endoproteases that deactivate the major membrane-active aurein peptides by removing residues from both the N- and C-termini of the peptides. The most abundant degradation products have two residues missing from the N-terminal end of the peptide. The solution structure of the basic peptide, aurein 1.2, has been determined by NMR spectroscopy to be an amphipathic alpha-helix with well-defined hydrophilic and hydrophobic regions. Certain of the aurein peptides (e.g. aureins 1.2 and 3.1) show anticancer activity in the NCI test regime, with LC50 values in the 10-5-10-4 M range. The aurein 1 peptides have only 13 amino-acid residues: these are the smallest antibiotic and anticancer active peptides yet reported from an anuran. The longer aurein 4 and 5 peptides, e.g. aurein 4.1 (GLIQTIKEKLKELAGGLVTGIQS-OH) and aurein 5. 1 (GLLDIVTGLLGNLIVDVLKPKTPAS-OH) show neither antibacterial nor anticancer activity.