Peptide name : Maculatin 1.1

Source/Organism : Skin secretions, Fringed Tree Frog, Australia

Linear/Cyclic : Not found

Chirality : L

Peptide length: 22

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 : 2245.6629 Dalton

Aliphatic index : 1.418

Instability index : 7.3364

Hydrophobicity (GRAVY) : 1.4318

Isoelectric point : 6.9209

Charge (pH 7) : -0.0637

Aromaticity : 0.090

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

Hydrophobic/hydrophilic ratio : 4.5

hydrophobic moment : -0.138

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

Most occurring amino acid : V

Most occurring amino acid frequency : 5

Least occurring amino acid : K

Least occurring amino acid frequency : 1

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

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](C)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(C)C)NC(=O)CN)C(C)C)C(C)C)C(C)C)C(C)C)C(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](Cc1ccccc1)C(=O)O

1 : Rozek T, et al. The maculatin peptides from the skin glands of the tree frog Litoria genimaculata: a comparison of the structures and antibacterial activities of maculatin 1.1 and caerin 1.1. J Pept Sci. 1998; 4:111-5. doi: 10.1002/(sici)1099-1387(199804)4:2<111::aid-psc134>3.0.co;2-8

Paper title : The maculatin peptides from the skin glands of the tree frog Litoria genimaculata: a comparison of the structures and antibacterial activities of maculatin 1.1 and caerin 1.1.

Doi : https://doi.org/10.1002/(sici)1099-1387(199804)4:2<111::aid-psc134>3.0.co;2-8

Abstract : Six peptides have been isolated and characterized from the dorsal glands of the tree frog Litoria genimaculata. One of these is the known hypotensive peptide caerulein; the others have been named maculatins. The amino acid sequences of the maculatin peptides have been determined using a combination of fast atom bombardment mass spectrometry and automated Edman sequencing. Four of the maculatin peptides show antibiotic activity, with maculatin 1.1 [GLFGVLAKVAAHVVPAIAEHF(NH2)] showing the most pronounced activity, particularly against gram-positive organisms. Maculatin 1.1 resembles the known caerin 1 antibiotic peptides, except that four of the central amino acid residues (of the caerin 1 system) are missing in maculatin 1.1. A comparison of the antibiotic activity of maculatin 1.1 with those of caerin 1.1 is reported.