dbacp05220
General Description
Peptide name : PE-BBI
Source/Organism : Edible frog
Linear/Cyclic : Cyclic
Chirality : Not found
Sequence Information
Sequence : GALKGCWTKSIPPKPC
Peptide length: 16
C-terminal modification: Cyclic
N-terminal modification : Amidation
Non-natural peptide information: None
Activity Information
Assay type : MTT assay
Assay time : 24h
Activity : IC50 : 50.2 µM
Cell line : HKE3
Cancer type : Human colorectal cancer
Other activity : Not found
Physicochemical Properties
Amino acid composition bar chart :
Molecular mass : 1686.0504 Dalton
Aliphatic index : 0.55
Instability index : -0.325
Hydrophobicity (GRAVY) : -0.287
Isoelectric point : 9.3902
Charge (pH 7) : 2.7373
Aromaticity : 0.062
Molar extinction coefficient (cysteine, cystine): (5500, 5625)
Hydrophobic/hydrophilic ratio : 2.2
hydrophobic moment : -0.340
Missing amino acid : R,H,Q,M,E,F,D,Y,N,V
Most occurring amino acid : K
Most occurring amino acid frequency : 3
Least occurring amino acid : A
Least occurring amino acid frequency : 1
Structural Information
3D structure :
Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.3, 0.2)
SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CS)NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)CN)[C@@H](C)O)C(=O)N1CCC[C@H]1C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CS)C(=O)O
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | THHTTEECTCCCCCCC |
| Chou-Fasman (CF) | CCCCEEEECCCCCCCC |
| Neural Network (NN) | CCCCCCCCCCCCCCCC |
| Joint/Consensus | CCCCCEECCCCCCCCC |
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 : Lyu P, et al. Identification and pharmaceutical evaluation of novel frog skin-derived serine proteinase inhibitor peptide-PE-BBI (Pelophylax esculentus Bowman-Birk inhibitor) for the potential treatment of cancer. Sci Rep. 2018; 8:14502. doi: 10.1038/s41598-018-32947-5
Literature
Paper title : Identification and pharmaceutical evaluation of novel frog skin-derived serine proteinase inhibitor peptide-PE-BBI (Pelophylax esculentus Bowman-Birk inhibitor) for the potential treatment of cancer.
Doi : https://doi.org/10.1038/s41598-018-32947-5
Abstract : Amphibian venom-derived peptides have high potential in the field of anticancer drug discovery. We have isolated a novel Bowman-Birk proteinase inhibitor (BBI)-type peptide from the skin secretion of Pelophylax esculentus (PE) named PE-BBI, and evaluated its bio-functions and anti-cancer activity in vitro. PE-BBI is a heptadecapeptide with C-terminal amidation. The mRNA sequence and primary structure of PE-BBI were identified using RT-PCR and LC/MS, respectively. A trypsin inhibitory assay was used to characterize the serine proteinase inhibitory activity of synthetic PE-BBI. PE-BBI's myotropic activity was analyzed using isolated rat bladder and rat-tail artery smooth muscle tissues, and the anti-cancer ability of PE-BBI using human colorectal cancer cells. PE-BBI's mechanism of action was investigated using Discovery studio software. PE-BBI showed trypsin inhibitory activity (K<sub>i</sub> = 310 ± 72 nM), strong myotropic activity, and cytotoxicity that were specific to cancer cells, and no side effect to normal epithelial cells. The docking stimulation showed that PE-BBI had high affinity to several members of human kallikrein related peptidase (KLK) family. This finding helps to enrich our understanding of BBI peptides' mode of action. Moreover, the data presented here validates frog secretions as sources of potential novel proteinase inhibitors for cancer treatment.