Peptide name : Short α-helical peptide

Source/Organism : Alpha-helical proteins

Linear/Cyclic : Linear

Chirality : L

Peptide length: 14

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : MTT/MTS assay

Assay time : 24h

Activity : 90% Cytotoxicity at 4µM approx.

Cell line : HL-60

Cancer type : Leukemia cancer

Other activity : Anti-microbial

Amino acid composition bar chart :

Molecular mass : 1636.2036 Dalton

Aliphatic index : 1.95

Instability index : -33.164

Hydrophobicity (GRAVY) : 0.55

Isoelectric point : 10.699

Charge (pH 7) : 5.7541

Aromaticity : 0

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

Hydrophobic/hydrophilic ratio : 1.33333333

hydrophobic moment : -2.090

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 : 7

Least occurring amino acid : G

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.4, 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](CCCCN)NC(=O)[C@H](CCCCN)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@@H](C)CC)C(=O)O

1 : Chen C, et al. Molecular mechanisms of anticancer action and cell selectivity of short α-helical peptides. Biomaterials. 2014; 35:1552-61. doi: 10.1016/j.biomaterials.2013.10.082

Paper title : Molecular mechanisms of anticancer action and cell selectivity of short α-helical peptides.

Doi : https://doi.org/10.1016/j.biomaterials.2013.10.082

Abstract : Development of functional biomaterials and drugs with good biocompatibility towards host cells but with high potency against cancer cells is a challenging endeavor. By drawing upon the advantageous features of natural antimicrobial peptides and α-helical proteins, we have designed a new class of short α-helical peptides G(IIKK)(n)I-NH2 (n = 1-4) with different potency and high selectivity against cancer cells. We show that the peptides with n = 3 and 4 kill cancer cells effectively whilst remaining benign to the host cells at their working concentrations, through mechanistic processes similar to their bactericidal effects. The high cell selectivity could stem from their preferential binding to the outer cell membranes containing negative charges and high fluidity. In addition to rapid membrane-permeabilizing capacities, the peptides can also induce the programmed cell death of cancer cells via both mitochondrial pathway and death receptor pathway, without inducing non-specific immunogenic responses. Importantly, these peptides can also inhibit tumor growth in a mouse xenograft model without eliciting side effects. Whilst this study reveals the clinical potential of these peptides as potent drugs and for other medical and healthcare applications, it also points to the significance of fundamental material research in the future development of highly selective peptide functional materials.