Peptide name : P18 (Cecropin A(1-8)-Magainin 2(1ˆ’12) hybrid peptide Analogue)

Source/Organism : Synthetic construct

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 18

C-terminal modification: Not found

N-terminal modification : Not found

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 activity

Amino acid composition bar chart :

Molecular mass : 2300.9155 Dalton

Aliphatic index : 0.922

Instability index : -9.9389

Hydrophobicity (GRAVY) : -0.383

Isoelectric point : 10.778

Charge (pH 7) : 6.8403

Aromaticity : 0.222

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

Hydrophobic/hydrophilic ratio : 1.25

hydrophobic moment : 1.2282

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

Most occurring amino acid : K

Most occurring amino acid frequency : 7

Least occurring amino acid : W

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.6, 0.0, 0.4)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@@H](N)CCCCN)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](Cc1ccccc1)C(=O)O

1 : Lee SH, et al. Antibiotic activity of reversed peptides of alpha-helical antimicrobial peptide, P18. Protein Pept Lett. 2002; 9:395-402. doi: 10.2174/0929866023408535

Paper title : Antibiotic activity of reversed peptides of alpha-helical antimicrobial peptide, P18.

Doi : https://doi.org/10.2174/0929866023408535

Abstract : P18 (KWKLFKKIPKFLHLAKKF-NH(2)), an a-helical antimicrobial peptide designed from cecropin Amagainin 2 hybrid, was known to have potent antimicrobial activity against bacteria as well as fungi without hemolytic activity. To find the peptides comparable or superior to the antimicrobial activity of P18, the two reversed peptides (Rev-1 and Rev-2) of P18 were designed and synthesized. These peptides were found to have similar antimicrobial activity against bacterial and fungal cells without hemolytic activity as compared with P18. Furthermore, a reversed peptide, Rev-2 was shown to have a two-fold higher activity in killing some bacterial cells than P18. Therefore, these results suggested that Rev-2 peptide seems to be an excellent candidate for developing novel peptide antibiotics.