Peptide name : Adenoregulin

Source/Organism : South American frog, Giant leaf frog

Linear/Cyclic : Linear

Chirality : L

Peptide length: 33

C-terminal modification: Linear

N-terminal modification : Free

Non-natural peptide information: None

Assay type : LDH leakage assay

Assay time : 24h

Activity : GI50 : 1.24 ± 0.23 µM

Cell line : PC-3

Cancer type : Prostate cancer

Other activity : Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 3181.6835 Dalton

Aliphatic index : 0.951

Instability index : 7.2727

Hydrophobicity (GRAVY) : 0.197

Isoelectric point : 9.701

Charge (pH 7) : 2.7625

Aromaticity : 0.030

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

Hydrophobic/hydrophilic ratio : 2

hydrophobic moment : -0.718

Missing amino acid : C,R,H,Q,T,P,M,F,D,Y,N

Most occurring amino acid : A

Most occurring amino acid frequency : 11

Least occurring amino acid : W

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.6, 0.1, 0.2)

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

1 : van Zoggel H, et al. Antitumor and angiostatic activities of the antimicrobial peptide dermaseptin B2. PLoS One. 2012; 7:e44351. doi: 10.1371/journal.pone.0044351

Paper title : Antitumor and angiostatic activities of the antimicrobial peptide dermaseptin B2.

Doi : https://doi.org/10.1371/journal.pone.0044351

Abstract : Recently, we have found that the skin secretions of the Amazonian tree frog Phyllomedusa bicolor contains molecules with antitumor and angiostatic activities and identified one of them as the antimicrobial peptide dermaseptin (Drs) B2. In the present study we further explored the in vitro and in vivo antitumor activity of this molecule and investigated its mechanism of action. We showed that Drs B2 inhibits the proliferation and colony formation of various human tumor cell types, and the proliferation and capillary formation of endothelial cells in vitro. Furthermore, Drs B2 inhibited tumor growth of the human prostate adenocarcinoma cell line PC3 in a xenograft model in vivo. Research on the mechanism of action of Drs B2 on tumor PC3 cells demonstrated a rapid increasing amount of cytosolic lactate dehydrogenase, no activation of caspase-3, and no changes in mitochondrial membrane potential. Confocal microscopy analysis revealed that Drs B2 can interact with the tumor cell surface, aggregate and penetrate the cells. These data together indicate that Drs B2 does not act by apoptosis but possibly by necrosis. In conclusion, Drs B2 could be considered as an interesting and promising pharmacological and therapeutic leader molecule for the treatment of cancer.