Peptide name : ZXR-1

Source/Organism : Venom base

Linear/Cyclic : Linear

Chirality : L

Peptide length: 16

C-terminal modification: Linear

N-terminal modification : Not found

Non-natural peptide information: None

Assay type : MTT assay

Assay time : 4h

Activity : IC50 : 141.7 ± 12.2 µM

Cell line : HepG2

Cancer type : Not found

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 1892.3359 Dalton

Aliphatic index : 1.037

Instability index : 28.7312

Hydrophobicity (GRAVY) : 0.0875

Isoelectric point : 11.333

Charge (pH 7) : 4.7561

Aromaticity : 0.187

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

Hydrophobic/hydrophilic ratio : 1.66666666

hydrophobic moment : -0.686

Missing amino acid : C,H,Q,T,P,M,E,D,Y,N,V

Most occurring amino acid : K

Most occurring amino acid frequency : 4

Least occurring amino acid : W

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.4, 0.1, 0.4)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)Cc1ccccc1)C(=O)NCC(=O)NCC(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)O)[C@@H](C)CC

1 : Zhou XR, et al. From a pro-apoptotic peptide to a lytic peptide: One single residue mutation. Biochim Biophys Acta. 2016; 1858:1914-25. doi: 10.1016/j.bbamem.2016.05.012

Paper title : From a pro-apoptotic peptide to a lytic peptide: One single residue mutation.

Doi : https://doi.org/10.1016/j.bbamem.2016.05.012

Abstract : Further discovery and design of new anticancer peptides are important for the development of anticancer therapeutics, and study on the detailed acting mechanism and structure-function relationship of peptides is critical for anticancer peptide design and application. In this study, a novel anticancer peptide ZXR-1 (FKIGGFIKKLWRSKLA) derived from a known anticancer peptide mauriporin was developed, and a mutant ZXR-2 (FKIGGFIKKLWRSLLA) with only one residue difference at the 14th position (Lys→Leu) was also engineered. Replacement of the lysine with leucine made ZXR-2 more potent than ZXR-1 in general. Even with only one residue mutation, the two peptides displayed distinct anticancer modes of action. ZXR-1 could translocate into cells, target on the mitochondria and induce cell apoptosis, while ZXR-2 directly targeted on the cell membranes and caused membrane lysis. The variance in their acting mechanisms might be due to the different amphipathicity and positive charge distribution. In addition, the two Ile-Leu pairs (3-10 and 7-14) in ZXR-2 might also play a role in improving its cytotoxicity. Further study on the structure-function relationship of the two peptides may be beneficial for the design of novel anticancer peptides and peptide based therapeutics.