Peptide name : Pleurocidin

Source/Organism : The skin mucous secretions, Winter flounder, PWinter flounder

Linear/Cyclic : Linear

Chirality : L

Peptide length: 25

C-terminal modification: Linear

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 : 2711.1283 Dalton

Aliphatic index : 0.704

Instability index : 4.972

Hydrophobicity (GRAVY) : -0.068

Isoelectric point : 10.176

Charge (pH 7) : 4.0166

Aromaticity : 0.16

Molar extinction coefficient (cysteine, cystine): (6990, 6990)

Hydrophobic/hydrophilic ratio : 1.5

hydrophobic moment : -0.079

Missing amino acid : C,R,Q,P,M,I,E,D,N

Most occurring amino acid : G

Most occurring amino acid frequency : 4

Least occurring amino acid : W

Least occurring amino acid frequency : 1

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

SMILES Notation: CC(C)C[C@H](NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)CN)C(C)C)C(C)C)[C@@H](C)O)C(=O)O

1 : Cole AM, et al. Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder. J Biol Chem. 1997; 272:12008-13. doi: 10.1074/jbc.272.18.12008

Paper title : Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder.

Doi : https://doi.org/10.1074/jbc.272.18.12008

Abstract : Antimicrobial peptides are found in both myeloid cells and mucosal tissues of many vertebrates and invertebrates. These peptides are predicted to operate as a first-line host defense mechanism exerting broad-spectrum activity against pathogenic bacteria, fungi, parasites, and enveloped viruses. We report the characterization of a novel 25-residue linear antimicrobial peptide found in the skin mucous secretions of the winter flounder (Pleuronectes americanus). This peptide was purified through multiple chromatographic methods to obtain a single peak by reversed-phase high performance liquid chromatography. This purified peptide, which we named pleurocidin, exhibited antimicrobial activity against Escherichia coli in a bacterial cell lysis plate assay. Mass spectrometry and amino acid sequence analysis indicated that it is 25 amino acids in length. Pleurocidin is predicted to assume an amphipathic alpha-helical conformation similar to many other linear antimicrobial peptides. There is a high degree of homology between pleurocidin and two antimicrobial peptides, ceratotoxin from the Mediterranean fruit fly and dermaseptin from the skin of a hylid frog. The minimal inhibitory concentration and minimal bactericidal concentration of pleurocidin were determined against 11 different Gram-negative and Gram-positive bacteria. Immunohistochemistry locates pleurocidin in the epithelial mucous cells of flounder skin. Pleurocidin represents a novel antimicrobial peptide found in fish and may play a role in innate host defense.