Peptide name : NRC-03

Source/Organism : PWinter flounder

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 26

C-terminal modification: Not found

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : MIC assay

Assay time : 24h

Activity : MIC : 1 - 8µg/ml

Cell line : Not found

Cancer type : Not found

Other activity : Anti- microbial activity

Amino acid composition bar chart :

Molecular mass : 2955.5585 Dalton

Aliphatic index : 1.088

Instability index : 68.9462

Hydrophobicity (GRAVY) : -0.576

Isoelectric point : 12

Charge (pH 7) : 7.8444

Aromaticity : 0.038

Molar extinction coefficient (cysteine, cystine): (5500, 5500)

Hydrophobic/hydrophilic ratio : 1.36363636

hydrophobic moment : 0.7115

Missing amino acid : C,Q,T,P,M,E,F,S,Y,N

Most occurring amino acid : G

Most occurring amino acid frequency : 5

Least occurring amino acid : W

Least occurring amino acid frequency : 1

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

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCCNC(=N)N)NC(=O)CN)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@H](C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](CC(C)C)C(=O)O)[C@@H](C)CC)[C@@H](C)CC)C(C)C

1 : Patrzykat A, et al. Novel antimicrobial peptides derived from flatfish genes. Antimicrob Agents Chemother. 2003; 47:2464-70. doi: 10.1128/AAC.47.8.2464-2470.2003

Paper title : Novel antimicrobial peptides derived from flatfish genes.

Doi : https://doi.org/10.1128/AAC.47.8.2464-2470.2003

Abstract : We report on the identification of active novel antimicrobials determined by screening both the genomic information and the mRNA transcripts from a number of different flatfish for sequences encoding antimicrobial peptides, predicting the sequences of active peptides from the genetic information, producing the predicted peptides chemically, and testing them for their activities. We amplified 35 sequences from various species of flatfish using primers whose sequences are based on conserved flanking regions of a known antimicrobial peptide from winter flounder, pleurocidin. We analyzed the sequences of the amplified products and predicted which sequences were likely to encode functional antimicrobial peptides on the basis of charge, hydrophobicity, relation to flanking sequences, and similarity to known active peptides. Twenty peptides were then produced synthetically and tested for their activities against gram-positive and gram-negative bacteria and the yeast Candida albicans. The most active peptide (with the carboxy-terminus amidated sequence GWRTLLKKAEVKTVGKLALKHYL, derived from American plaice) showed inhibitory activity over a concentration range of 1 to 8 micro g/ml against a test panel of pathogens, including the intrinsically antibiotic-resistant organism Pseudomonas aeruginosa, methicillin-resistant Staphylococcus aureus, and C. albicans. The methods described here will be useful for the identification of novel peptides with good antimicrobial activities.