Peptide name : SVS-1

Source/Organism : Bovine lactoferrin (Lf-B)

Linear/Cyclic : Linear

Chirality : Mix

Peptide length: 18

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : MTT/MTS assay

Assay time : 24h

Activity : Not found

Cell line : KB

Cancer type : Oral cancer

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 2032.645 Dalton

Aliphatic index : 1.127

Instability index : -11.772

Hydrophobicity (GRAVY) : -0.316

Isoelectric point : 10.845

Charge (pH 7) : 7.7521

Aromaticity : 0

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

Hydrophobic/hydrophilic ratio : 0.88888888

hydrophobic moment : -0.137

Missing amino acid : C,R,W,H,Q,M,I,E,F,S,D,Y,L,N,A,G

Most occurring amino acid : K

Most occurring amino acid frequency : 8

Least occurring amino acid : p

Least occurring amino acid frequency : 1

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

SMILES Notation: CC(C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@@H](N)CCCCN)C(C)C)C(C)C)C(C)C)C(C)C)[C@@H](C)O)C(C)C)C(C)C)C(=O)N[C@@H](CCCCN)C(=O)O

1 : Sinthuvanich C, et al. Anticancer β-hairpin peptides: membrane-induced folding triggers activity. J Am Chem Soc. 2012; 134:6210-7. doi: 10.1021/ja210569f

Paper title : Anticancer β-hairpin peptides: membrane-induced folding triggers activity.

Doi : https://doi.org/10.1021/ja210569f

Abstract : Several cationic antimicrobial peptides (AMPs) have recently been shown to display anticancer activity via a mechanism that usually entails the disruption of cancer cell membranes. In this work, we designed an 18-residue anticancer peptide, SVS-1, whose mechanism of action is designed to take advantage of the aberrant lipid composition presented on the outer leaflet of cancer cell membranes, which makes the surface of these cells electronegative relative to the surface of noncancerous cells. SVS-1 is designed to remain unfolded and inactive in aqueous solution but to preferentially fold at the surface of cancer cells, adopting an amphiphilic β-hairpin structure capable of membrane disruption. Membrane-induced folding is driven by electrostatic interaction between the peptide and the negatively charged membrane surface of cancer cells. SVS-1 is active against a variety of cancer cell lines such as A549 (lung carcinoma), KB (epidermal carcinoma), MCF-7 (breast carcinoma), and MDA-MB-436 (breast carcinoma). However, the cytotoxicity toward noncancerous cells having typical membrane compositions, such as HUVEC and erythrocytes, is low. CD spectroscopy, appropriately designed peptide controls, cell-based studies, liposome leakage assays, and electron microscopy support the intended mechanism of action, which leads to preferential killing of cancerous cells.