Peptide name : Citropin 1.1

Source/Organism : Skin secretion, Australian blue mountains tree frog

Linear/Cyclic : Not found

Chirality : L

Peptide length: 16

C-terminal modification: Not found

N-terminal modification : Free

Non-natural peptide information: None

Assay type : Not specified

Assay time : 24h

Activity : Not found

Cell line : Not found

Cancer type : Not found

Other activity : Anti-bacterial activity

Amino acid composition bar chart :

Molecular mass : 1615.9536 Dalton

Aliphatic index : 1.581

Instability index : 14.1875

Hydrophobicity (GRAVY) : 1.2813

Isoelectric point : 8.5909

Charge (pH 7) : 0.7592

Aromaticity : 0.062

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

Hydrophobic/hydrophilic ratio : 3

hydrophobic moment : -0.312

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

Most occurring amino acid : G

Most occurring amino acid frequency : 3

Least occurring amino acid : F

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.3, 0.5)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=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(C)C)[C@@H](C)CC)C(C)C)C(C)C)C(=O)NCC(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)O

1 : Wegener KL, et al. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1. Eur J Biochem. 1999; 265:627-37. doi: 10.1046/j.1432-1327.1999.00750.x

Paper title : Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1.

Doi : https://doi.org/10.1046/j.1432-1327.1999.00750.x

Abstract : Nineteen citropin peptides are present in the secretion from the granular dorsal glands of the Blue Mountains tree-frog Litoria citropa; 15 of these peptides are also present in the secretion from the submental gland. Two major peptides, citropin 1.1 (GLFDVIKKVASVIGGL-NH2), citropin 1.2 (GLFDIIKKVASVVGGL-NH2) and a minor peptide, citropin 1.3 (GLFDIIKKVASVIGGL-NH2) are wide-spectrum antibacterial peptides. The amphibian has an endoprotease which deactivates these membrane-active peptides by removing residues from the N-terminal end: loss of three residues gives the most abundant degradation products. The solution structure of the basic peptide citropin 1.1 has been determined by NMR spectroscopy [in a solvent mixture of trifluoroethanol/water (1 : 1)] to be an amphipathic alpha-helix with well-defined hydrophobic and hydrophilic regions. The additional four peptides produced by the dorsal glands are structurally related to the antibacterial citropin 1 peptides but contain three more residues at their C-terminus [e.g. citropin 1.1.3 (GLFDVIKKVASVIGLASP-OH)]. These peptides show minimal antibacterial activity; their role in the amphibian skin is not known.