Peptide name : Indolicidin

Source/Organism : Cattle neutrophils

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 13

C-terminal modification: Not found

N-terminal modification : Carboxyl-terminal arginine was carboxamidated

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 : Not found

Amino acid composition bar chart :

Molecular mass : 1907.2693 Dalton

Aliphatic index : 0.6

Instability index : 76.2769

Hydrophobicity (GRAVY) : -1.069

Isoelectric point : 12

Charge (pH 7) : 2.7591

Aromaticity : 0.384

Molar extinction coefficient (cysteine, cystine): (27500, 27500)

Hydrophobic/hydrophilic ratio : 3.33333333

hydrophobic moment : 0.143

Missing amino acid : C,H,Q,T,M,E,F,S,D,Y,N,A,V,G

Most occurring amino acid : W

Most occurring amino acid frequency : 5

Least occurring amino acid : I

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.1, 0.2, 0.5)

SMILES Notation: CC[C@H](C)[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N1CCC[C@H]1C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N1CCC[C@H]1C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)O

1 : Selsted ME, et al. Indolicidin, a novel bactericidal tridecapeptide amide from neutrophils. J Biol Chem. 1992; 267:4292-5.

Paper title : Indolicidin, a novel bactericidal tridecapeptide amide from neutrophils.

Doi : https://doi.org/Not available

Abstract : A potent and structurally novel antimicrobial peptide was purified from the cytoplasmic granules of bovine neutrophils. Suspensions of Staphylococcus aureus and Escherichia coli were virtually sterilized by the peptide at a concentration of 10 micrograms/ml. The peptide was found to be comprised of 13 amino acids, 5 of which were tryptophan residues, and the carboxyl-terminal arginine was carboxamidated. The primary structure of the peptide, which we have named indolicidin, is H-Ile-Leu-Pro-Trp-Lys-Trp-Pro-Trp-Trp-Pro-Trp-Arg-Arg-NH2. The mole percent of tryptophan in indolicidin is the highest observed among known protein sequences. The multiple tryptophan residues presumably play an important role in the function of this unique antibiotic peptide.