dbacp03352
General Description
Peptide name : Hymenochirin-1B
Source/Organism : Zaire dwarf clawed frog
Linear/Cyclic : Not found
Chirality : Not found
Sequence Information
Sequence : KLSPETKDNLKKVLKGAIKGAIVAKMV
Peptide length: 27
C-terminal modification: Not found
N-terminal modification : Not found
Non-natural peptide information: None
Activity Information
Assay type : Cytotoxicity assay, Cell TiterGlo Luminescent Cell viability assay
Assay time : 24h
Activity : LC50 : 2.5 ± 0.2 μM
Cell line : A549
Cancer type : Lung cancer
Other activity : Not found
Physicochemical Properties
Amino acid composition bar chart :
Molecular mass : 2880.5351 Dalton
Aliphatic index : 1.155
Instability index : 12.9704
Hydrophobicity (GRAVY) : -0.051
Isoelectric point : 10.125
Charge (pH 7) : 4.757
Aromaticity : 0
Molar extinction coefficient (cysteine, cystine): (0, 0)
Hydrophobic/hydrophilic ratio : 1.25
hydrophobic moment : -0.906
Missing amino acid : C,R,W,H,Q,F,Y
Most occurring amino acid : K
Most occurring amino acid frequency : 7
Least occurring amino acid : S
Least occurring amino acid frequency : 1
Structural Information
3D structure :
Secondary structure fraction (Helix, Turn, Sheet): (0.5, 0.2, 0.3)
SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](C)NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CCCCN)[C@@H](C)O)C(C)C)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCSC)C(=O)N[C@H](C(=O)O)C(C)C)C(C)C)[C@@H](C)CC
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | TCCCTHHHHHHHHHHHHHHHHHHHHHH |
| Chou-Fasman (CF) | CCCCCCHHHHHHCHHHHHHEEECCCCC |
| Neural Network (NN) | CCCCCCCCHHHHHHHHHHCHHHHHHHH |
| Joint/Consensus | CCCCCCHHHHHHHHHHHHHHHHHHHHH |
Molecular Descriptors and ADMET Properties
Molecular Descriptors: Click here to download
ADMET Properties: Click here to download
Cross Referencing databases
CancerPPD : Not available
ApIAPDB : Not available
CancerPPD2 ID : Not available
Reference
1 : Attoub S, et al. Anti-tumor activities of the host-defense peptide hymenochirin-1B. Regul Pept. 2013; 187:51-6. doi: 10.1016/j.regpep.2013.10.006
Literature
Paper title : Anti-tumor activities of the host-defense peptide hymenochirin-1B.
Doi : https://doi.org/10.1016/j.regpep.2013.10.006
Abstract : The hymenochirins are a family of cationic, amphipathic, α-helical host-defense peptides, first isolated from skin secretions of the Congo clawed frog Hymenochirus boettgeri (Pipidae). Of the four hymenochirins tested, hymenochirin-1B (IKLSPETKDNLKKVLKGAIKGAIVAKMV.NH2) shows the greatest cytotoxic potency against non-small cell lung adenocarcinoma A549 cells (LC50=2.5±0.2 μM), breast adenocarcinoma MDA-MB-231 cells (LC50=9.0±0.3 μM), colorectal adenocarcinoma HT-29 cells (LC50=9.7±0.2 μM), and hepatocarcinoma HepG2 cells (LC50=22.5±1.4 μM) with appreciably less hemolytic activity against human erythrocytes (LC50=213±18μM). Structure-activity relationships were investigated by synthesizing analogs of hymenochirin-1B in which Pro(5), Glu(6) and Asp(9)on the hydrophilic face of the helix were replaced by one or more L-lysine or D-lysine residues. The [D9K] analog displays the greatest increase in potency against all four cell lines (up to 6 fold) but hemolytic activity also increases (LC50=174±12 μM). The [D9k] and [E6k,D9k] analogs retain relatively high cytotoxic potency against the tumor cells (LC50 in the range 2.1-21 μM) but show reduced hemolytic activity (LC50>300 μM). The data suggest that hymenochirin-1B has therapeutic potential as a template to generate potent, non-toxic anti-cancer agents.