Peptide name : Cationic Amphiphilic

Source/Organism : AMP

Linear/Cyclic : Cyclic

Chirality : L

Peptide length: 11

C-terminal modification: Cyclic

N-terminal modification : Free

Non-natural peptide information: None

Assay type : WST-1 assay

Assay time : Not found

Activity : IC50 : >500 µM

Cell line : HL-60

Cancer type : Pancreatic cancer

Other activity : Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 1266.7014 Dalton

Aliphatic index : 2.127

Instability index : -29.5

Hydrophobicity (GRAVY) : 1

Isoelectric point : 10.477

Charge (pH 7) : 3.7561

Aromaticity : 0

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

Hydrophobic/hydrophilic ratio : 1.75

hydrophobic moment : -0.710

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

Most occurring amino acid : I

Most occurring amino acid frequency : 6

Least occurring amino acid : G

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.0, 0.5)

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

1 : Hu J, et al. Designed antimicrobial and antitumor peptides with high selectivity. Biomacromolecules. 2011; 12:3839-43. doi: 10.1021/bm201098j

Paper title : Designed antimicrobial and antitumor peptides with high selectivity.

Doi : https://doi.org/10.1021/bm201098j

Abstract : We report a new class of cationic amphiphilic peptides with short sequences, G(IIKK)(n)I-NH(2) (n = 1-4), that can kill Gram-positive and Gram-negative bacteria as effectively as several well-known antimicrobial peptides and antibiotics. In addition, some of these peptides possess potent antitumor activities against cancer cell lines. Moreover, their hemolytic activities against human red blood cells (hRBCs) remain remarkably low even at some 10-fold bactericidal minimum inhibitory concentrations (MICs). When bacteria or tumor cells are cocultured with NIH 3T3 fibroblast cells, G(IIKK)(3)I-NH(2) showed fast and strong selectivity against microbial or tumor cells, without any adverse effect on NIH 3T3 cells. The high selectivity and associated features are attributed to two design tactics: the use of Ile residues rather than Leu and the perturbation of the hydrophobic face of the helical structure with the insertion of a positively charged Lys residue. This class of simple peptides hence offers new opportunities in the development of cost-effective and highly selective antimicrobial and antitumor peptide-based treatments.