Peptide name : Temporin-Las

Source/Organism : Temporins family

Linear/Cyclic : Linear

Chirality : L

Peptide length: 13

C-terminal modification: Linear

N-terminal modification : Free

Non-natural peptide information: None

Assay type : MTT/MTS assay

Assay time : 24h

Activity : 55.98 inhibition ratio at 50 µg/ml

Cell line : HepG-2

Cancer type : Liver cancer

Other activity : Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 1581.9854 Dalton

Aliphatic index : 1.946

Instability index : 44.9308

Hydrophobicity (GRAVY) : 0.8077

Isoelectric point : 10.289

Charge (pH 7) : 2.8443

Aromaticity : 0.076

Molar extinction coefficient (cysteine, cystine): (1490, 1490)

Hydrophobic/hydrophilic ratio : 1.16666666

hydrophobic moment : 0.7391

Missing amino acid : C,W,Q,T,P,M,E,F,D,N,A,G

Most occurring amino acid : L

Most occurring amino acid frequency : 4

Least occurring amino acid : R

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.4, 0.0, 0.6)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CC(C)C)C(C)C)C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CC(C)C)C(=O)O

1 : Diao Y, et al. Designed synthetic analogs of the α-helical peptide temporin-La with improved antitumor efficacies via charge modification and incorporation of the integrin αvβ3 homing domain. J Pept Sci. 2012; 18:476-86. doi: 10.1002/psc.2420

Paper title : Designed synthetic analogs of the α-helical peptide temporin-La with improved antitumor efficacies via charge modification and incorporation of the integrin αvβ3 homing domain.

Doi : https://doi.org/10.1002/psc.2420

Abstract : How to target cancer cells with high specificity and kill cancer cells with high efficiency remains an urgent demand for anticancer drugs. Temporin-La, which belongs to the family of temporins, presents antitumor activity against many cancer cell lines. We first used a whole bioinformatic analysis method as a platform to identify new anticancer antimicrobial peptides (AMPs). On the basis of these results, we designed a temporin-La analog (temporin-Las) and related constructs containing the Arg-Gly-Asp (RGD) tripeptide, the integrin αvβ3 homing domain (RGD-La and RGD-Las). We detected a link between the net charges and integrin αvβ3 expression of cancer cell lines and the antitumor activities of these peptides. Temporin-La and its synthetic analogs inhibited cancer cell proliferation in a dose-dependent manner. Evidence was provided that the affinity between RGD-Las and tumor cell membranes was stronger than other tested peptides using a pull-down assay. Morphological changes on the cell membrane induced by temporin-La and RDG-Las, respectively, were examined by scanning electron microscopy. Additionally, time-dependent morphological changes were detected by confocal microscopy, where the binding process of RGD-Las to the cell membrane could be monitored. The results indicate that the electrostatic interaction between these cationic peptides and the anionic cell membrane is a major determinant of selective cell killing. Thus, the RGD tripeptide is a valuable ligand motif for tumor targeting, which leads to an increased anticancer efficiency by RGD-Las. These AMP-derived peptides have clinical potential as specifically targeting agents for the treatment of αvβ3 positive tumors.