Peptide name : Caerin 1.9

Source/Organism : Red-eyed tree frog, Australia

Linear/Cyclic : Not found

Chirality : L

Peptide length: 24

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-microbial; Anti-biotic activity

Amino acid composition bar chart :

Molecular mass : 2480.9867 Dalton

Aliphatic index : 1.5

Instability index : 33.6583

Hydrophobicity (GRAVY) : 1.0375

Isoelectric point : 8.6056

Charge (pH 7) : 0.9353

Aromaticity : 0.041

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

Hydrophobic/hydrophilic ratio : 3

hydrophobic moment : -1.112

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

Most occurring amino acid : V

Most occurring amino acid frequency : 5

Least occurring amino acid : F

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.2, 0.4)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(C)C)NC(=O)CN)C(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@H](C(=O)N[C@H](C(=O)N1CCC[C@H]1C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)O)[C@@H](C)CC)C(C)C)C(C)C)C(C)C)C(C)C

1 : Steinborner ST, et al. New antibiotic caerin 1 peptides from the skin secretion of the Australian tree frog Litoria chloris. Comparison of the activities of the caerin 1 peptides from the genus Litoria. J Pept Res. 1998; 51:121-6. doi: 10.1111/j.1399-3011.1998.tb00629.x

2 : Wang G, et al. APD2: the updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res. 2009; 37:D933-7. doi: 10.1093/nar/gkn823

Paper title : New antibiotic caerin 1 peptides from the skin secretion of the Australian tree frog Litoria chloris. Comparison of the activities of the caerin 1 peptides from the genus Litoria.

Doi : https://doi.org/10.1111/j.1399-3011.1998.tb00629.x

Abstract : The skin glands of the tree frog Litoria chloris contain a variety of peptides including four antibacterial peptides of the caerin 1 family. Two of these, caerins 1.6 and 1.7, are also present in the related species Litoria xanthomera. The other two peptides, caerins 1.8 and 1.9, are new. Their sequences are: GLFKVLGSVAKHLLPHVVPVIAEKL-NH2 [Caerin 1.8] and GLFGVLGSIAKHVLPHVVPVIAEKL-NH2 [Caerin 1.9]. Comparison of the skin peptide profiles of L. chloris and L. xanthomera confirms that these species are more closely related to each other than to any other species of the genus Litoria that we have studied. A comparison is made of the antibiotic activities of nine members of the caerin 1 family of peptides isolated from tree frogs of the genus Litoria.

Paper title : APD2: the updated antimicrobial peptide database and its application in peptide design.

Doi : https://doi.org/10.1093/nar/gkn823

Abstract : The antimicrobial peptide database (APD, http://aps.unmc.edu/AP/main.php) has been updated and expanded. It now hosts 1228 entries with 65 anticancer, 76 antiviral (53 anti-HIV), 327 antifungal and 944 antibacterial peptides. The second version of our database (APD2) allows users to search peptide families (e.g. bacteriocins, cyclotides, or defensins), peptide sources (e.g. fish, frogs or chicken), post-translationally modified peptides (e.g. amidation, oxidation, lipidation, glycosylation or d-amino acids), and peptide binding targets (e.g. membranes, proteins, DNA/RNA, LPS or sugars). Statistical analyses reveal that the frequently used amino acid residues (>10%) are Ala and Gly in bacterial peptides, Cys and Gly in plant peptides, Ala, Gly and Lys in insect peptides, and Leu, Ala, Gly and Lys in amphibian peptides. Using frequently occurring residues, we demonstrate database-aided peptide design in different ways. Among the three peptides designed, GLK-19 showed a higher activity against Escherichia coli than human LL-37.