Peptide name : Cecropin B

Source/Organism : Silkmoth

Linear/Cyclic : Linear

Chirality : L

Peptide length: 35

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : MTT/MTS assay

Assay time : 96h

Activity : IC50 : 24.5 µM

Cell line : MCF-7R

Cancer type : Breast cancer

Other activity : Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 3835.6542 Dalton

Aliphatic index : 1.06

Instability index : 35.4229

Hydrophobicity (GRAVY) : -0.071

Isoelectric point : 10.729

Charge (pH 7) : 6.7587

Aromaticity : 0.057

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

Hydrophobic/hydrophilic ratio : 1.69230769

hydrophobic moment : 0.8502

Missing amino acid : C,H,Q,T,S,D,Y

Most occurring amino acid : K

Most occurring amino acid frequency : 7

Least occurring amino acid : W

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.4, 0.2, 0.3)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)CNC(=O)[C@H](CCSC)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@@H](N)CCCCN)C(C)C)[C@@H](C)CC)[C@@H](C)CC)C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N1CCC[C@H]1C(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)O)C(C)C)[C@@H](C)CC)C(C)C

1 : Moore AJ, et al. Preliminary experimental anticancer activity of cecropins. Pept Res. 1994; 7:265-9.

Paper title : Preliminary experimental anticancer activity of cecropins.

Doi : https://doi.org/Not available

Abstract : The cecropins are a group of peptides that were first isolated from the hemolymph of the giant silk moth, Hyalophora cecropia. In preliminary studies, these novel peptides were shown to be active against several bacteria and mammalian lymphomas and leukemias in vitro. The mechanism of action of the cecropins is thought to involve pore formation at the cytoplasmic membrane. The potential anticancer activity of cecropin B, cecropin P1 and Shiva-1 was investigated against a panel of mammalian cell lines in vitro. Cell lines showed a range of sensitivities to cecropin B (IC50 3.2 to > 100 microM), and two cell lines with the multidrug-resistant phenotype were sensitive to the peptide. In vitro cecropin B activity was virtually complete within one hour. Preliminary in vivo studies showed that cecropin B increases the survival time of mice bearing murine ascitic colon adenocarcinoma cells. Future studies will address structure/activity relationships of similar peptides in order to optimize antitumor activity.