Peptide name : CRAMP-18 E2K

Source/Organism : Synthetic

Linear/Cyclic : Not found

Chirality : Not found

Peptide length: 18

C-terminal modification: Not found

N-terminal modification : Free

Non-natural peptide information: None

Assay type : MTT assay

Assay time : 72h

Activity : IC50 : 20–34 uM

Cell line : Jurkat

Cancer type : Acute T cell Leukemia

Other activity : Anti-bacterial activity; Hemolytic activity

Amino acid composition bar chart :

Molecular mass : 2146.663 Dalton

Aliphatic index : 0.866

Instability index : -31.922

Hydrophobicity (GRAVY) : -0.911

Isoelectric point : 10.778

Charge (pH 7) : 6.7531

Aromaticity : 0.111

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

Hydrophobic/hydrophilic ratio : 0.8

hydrophobic moment : 0.3683

Missing amino acid : C,R,W,H,T,P,M,E,S,D,Y,A,V

Most occurring amino acid : K

Most occurring amino acid frequency : 7

Least occurring amino acid : N

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.5, 0.1, 0.3)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)CN)C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)O)[C@@H](C)CC

1 : Shin SY, et al. CRAMP analogues having potent antibiotic activity against bacterial, fungal, and tumor cells without hemolytic activity. Biochem Biophys Res Commun. 2000; 275:904-9. doi: 10.1006/bbrc.2000.3269

Paper title : CRAMP analogues having potent antibiotic activity against bacterial, fungal, and tumor cells without hemolytic activity.

Doi : https://doi.org/10.1006/bbrc.2000.3269

Abstract : CRAMP-18 (GEKLKKIGQKIKNFFQKL) is the antibacterial sequence derived from CRMAP, a member of cathelicidin-derived antimicrobial peptides. To develop the novel antibiotic peptides useful as therapeutic drugs requires strong antibiotic activity against bacterial and fungal cells without hemolytic effect. To this goal, the analogues were designed to increase only net positively charge by Lys-substitution of positions 2, 9, 13, or 16 at the hydrophilic helix face of CRAMP-18 without any change at the hydrophobic helix face. In particular, Lys-substitution (K(2)-CRAMP-18) of position 2 in CRAMP-18 induced the enhanced antibiotic activity without any increase in hemolysis. Thus, this peptide may provide a useful template for the design novel antibiotic peptides for the treatment of infectious diseases. Additional CD spectra studies suggested that the alpha-helical structure of the peptides plays an important role in killing bacterial and fungal cells, but the increase of alpha-helical content is less connected with the enhanced antibiotic activity.