Peptide name : Dermaseptin-PD-1

Source/Organism : Skin Secretion, Mexican leaf frog, Mexico, North America

Linear/Cyclic : Cyclic

Chirality : Not found

Peptide length: 31

C-terminal modification: Cyclic

N-terminal modification : Free

Non-natural peptide information: None

Assay type : MTT assay

Assay time : 24h

Activity : IC50 : 15.08 μM

Cell line : U251MG

Cancer type : Human neuronal glioblastoma

Other activity : Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 3266.8526 Dalton

Aliphatic index : 0.635

Instability index : 10.329

Hydrophobicity (GRAVY) : -0.274

Isoelectric point : 9.701

Charge (pH 7) : 2.7608

Aromaticity : 0.032

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

Hydrophobic/hydrophilic ratio : 1.21428571

hydrophobic moment : -1.038

Missing amino acid : C,R,H,P,F,Y,L,N,V

Most occurring amino acid : A

Most occurring amino acid frequency : 8

Least occurring amino acid : W

Least occurring amino acid frequency : 1

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

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

1 : Shi D, et al. Two Novel Dermaseptin-Like Antimicrobial Peptides with Anticancer Activities from the Skin Secretion of Pachymedusa dacnicolor. Toxins (Basel). 2016; 8:(unknown pages). doi: 10.3390/toxins8050144

Paper title : Two Novel Dermaseptin-Like Antimicrobial Peptides with Anticancer Activities from the Skin Secretion of Pachymedusa dacnicolor.

Doi : https://doi.org/10.3390/toxins8050144

Abstract : The dermaseptin antimicrobial peptide family contains members of 27-34 amino acids in length that have been predominantly isolated from the skins/skin secretions of phyllomedusine leaf frogs. By use of a degenerate primer in Rapid amplification of cDNA ends (RACE) PCR designed to a common conserved domain within the 5'-untranslated regions of previously-characterized dermaseptin encoding cDNAs, two novel members of this peptide family, named dermaseptin-PD-1 and dermaseptin-PD-2, were identified in the skin secretion of the phyllomedusine frog, Pachymedusa dacnicolor. The primary structures of both peptides were predicted from cloned cDNAs, as well as being confirmed by mass spectral analysis of crude skin secretion fractions resulted from reversed-phase high-performance liquid chromatography. Chemically-synthesized replicates of dermaseptin-PD-1 and dermaseptin-PD-2 were investigated for antimicrobial activity using standard model microorganisms (Gram-positive bacteria, Gram-negative bacteria and a yeast) and for cytotoxicity using mammalian red blood cells. The possibility of synergistic effects between the two peptides and their anti-cancer cell proliferation activities were assessed. The peptides exhibited moderate to high inhibition against the growth of the tested microorganisms and cancer cell lines with low haemolytic activity. Synergistic interaction between the two peptides in inhibiting the proliferation of Escherichia coli and human neuronal glioblastoma cell line, U251MG was also manifested.