dbacp01861
General Description
Peptide name : Bombinin H-BO1
Source/Organism : Oriental Fire-bellied Toad
Linear/Cyclic : Not found
Chirality : Not found
Sequence Information
Sequence : IIGPVLGLVGKALGGLL
Peptide length: 17
C-terminal modification: Not found
N-terminal modification : Amidation
Non-natural peptide information: None
Activity Information
Assay type : MTT assay
Assay time : 48h
Activity : IC50 : 8.08 μM
Cell line : SK-HEP-1
Cancer type : Human hepatoma
Other activity : Not found
Physicochemical Properties
Amino acid composition bar chart :
Molecular mass : 1590.0024 Dalton
Aliphatic index : 2.005
Instability index : 18.0118
Hydrophobicity (GRAVY) : 1.8059
Isoelectric point : 8.7501
Charge (pH 7) : 0.7591
Aromaticity : 0
Molar extinction coefficient (cysteine, cystine): (0, 0)
Hydrophobic/hydrophilic ratio : 16
hydrophobic moment : 0.3497
Missing amino acid : C,R,W,H,Q,T,M,E,F,S,D,Y,N
Most occurring amino acid : G
Most occurring amino acid frequency : 5
Least occurring amino acid : P
Least occurring amino acid frequency : 1
Structural Information
3D structure :
Secondary structure fraction (Helix, Turn, Sheet): (0.4, 0.3, 0.5)
SMILES Notation: CC[C@H](C)[C@H](N)C(=O)N[C@H](C(=O)NCC(=O)N1CCC[C@H]1C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)O)C(C)C)C(C)C)[C@@H](C)CC
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | EECCEEEEEEEEETCEE |
| Chou-Fasman (CF) | EEEEEEEECCCCEECCC |
| Neural Network (NN) | CCCCCCHHHHHHCCCHH |
| Joint/Consensus | EECCEEEECCCCCCCCC |
Molecular Descriptors and ADMET Properties
Molecular Descriptors: Click here to download
ADMET Properties: Click here to download
Cross Referencing databases
Reference
1 : Peng X, et al. Molecular characterization and bioactivity evaluation of two novel bombinin peptides from the skin secretion of Oriental fire-bellied toad, Bombina orientalis. Amino Acids. 2018; 50:241-253. doi: 10.1007/s00726-017-2509-z
Literature
Paper title : Molecular characterization and bioactivity evaluation of two novel bombinin peptides from the skin secretion of Oriental fire-bellied toad, Bombina orientalis.
Doi : https://doi.org/10.1007/s00726-017-2509-z
Abstract : Following the exploration of biochemicals in amphibian defensive skin secretion, great attention has been focused on the novel bioactive peptides with unique molecular structures and complicated features and functions. In this study, the skin secretion of Oriental fire-bellied toad, Bombina orientalis, was acquired to search peptides with therapeutic potential. Using "shotgun" cloning technique, a full-length peptide precursor co-encoding two novel bombinin peptides was cloned from the skin secretion-derived cDNA library of B. orientalis. The deduced peptides were identified as one bombinin-like peptide (BLP) (GIGSAILSAGKSIIKGLAKGLAEHF-NH<sub>2</sub>) and one bombinin H-type peptide (BH) (IIGPVLGLVGKALGGLL-NH<sub>2</sub>). The primary structures of both peptides were confirmed through reverse-phase HPLC fractionation and mass spectrometry. Secondary structural prediction revealed Bombinin-BO1 and Bombinin H-BO1 adopted α-helical structural features. In addition, the two peptides exhibited broad-spectrum antimicrobial effect against Gram-positive and Gram-negative bacteria and yeast. Meanwhile, the anticancer activity assay indicated both peptides exerted significant anticancer effects against human hepatoma cell lines tested (Hep G2/SK-HEP-1/Huh7). The peptides reported here for the first time may represent novel lead compounds for the design/development of new therapeutics for human infection and neoplastic disease.