dbacp02637
General Description
Peptide name : Decoralin
Source/Organism : Solitary eumenine wasp
Linear/Cyclic : Not found
Chirality : Not found
Sequence Information
Sequence : SLLSLIRKLI
Peptide length: 10
C-terminal modification: Not found
N-terminal modification : Not found
Non-natural peptide information: None
Activity Information
Assay type : MTT assay
Assay time : 24h
Activity : IC50 : 12.5 μmolL−1
Cell line : MCF-7
Cancer type : Breast cancer
Other activity : Not found
Physicochemical Properties
Amino acid composition bar chart :
Molecular mass : 1155.4735 Dalton
Aliphatic index : 2.34
Instability index : 0.51
Hydrophobicity (GRAVY) : 1.42
Isoelectric point : 11.000
Charge (pH 7) : 1.4591
Aromaticity : 0
Molar extinction coefficient (cysteine, cystine): (0, 0)
Hydrophobic/hydrophilic ratio : 1.5
hydrophobic moment : -1.122
Missing amino acid : C,W,H,Q,T,P,M,E,F,D,Y,N,A,V,G
Most occurring amino acid : L
Most occurring amino acid frequency : 4
Least occurring amino acid : R
Least occurring amino acid frequency : 1
Structural Information
3D structure :
Secondary structure fraction (Helix, Turn, Sheet): (0.5, 0.2, 0.6)
SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CO)[C@@H](C)CC)C(=O)O
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | HHHHHHHEEE |
| Chou-Fasman (CF) | CCEECCCCCC |
| Neural Network (NN) | HHHHHHHHHH |
| Joint/Consensus | HHHHHHHCCC |
Molecular Descriptors and ADMET Properties
Molecular Descriptors: Click here to download
ADMET Properties: Click here to download
Cross Referencing databases
Reference
1 : Torres MDT, et al. Natural and redesigned wasp venom peptides with selective antitumoral activity. Beilstein J Org Chem. 2018; 14:1693-1703. doi: 10.3762/bjoc.14.144
Literature
Paper title : Natural and redesigned wasp venom peptides with selective antitumoral activity.
Doi : https://doi.org/10.3762/bjoc.14.144
Abstract : About 1 in 8 U.S. women (≈12%) will develop invasive breast cancer over the course of their lifetime. Surgery, chemotherapy, radiotherapy, and hormone manipulation constitute the major treatment options for breast cancer. Here, we show that both a natural antimicrobial peptide (AMP) derived from wasp venom (decoralin, Dec-NH<sub>2</sub>), and its synthetic variants generated via peptide design, display potent activity against cancer cells. We tested the derivatives at increasing doses and observed anticancer activity at concentrations as low as 12.5 μmol L-1 for the selective targeting of MCF-7 breast cancer cells. Flow cytometry assays further revealed that treatment with wild-type (WT) peptide Dec-NH<sub>2</sub> led to necrosis of MCF-7 cells. Additional atomic force microscopy (AFM) measurements indicated that the roughness of cancer cell membranes increased significantly when treated with lead peptides compared to controls. Biophysical features such as helicity, hydrophobicity, and net positive charge were identified to play an important role in the anticancer activity of the peptides. Indeed, abrupt changes in peptide hydrophobicity and conformational propensity led to peptide inactivation, whereas increasing the net positive charge of peptides enhanced their activity. We present peptide templates with selective activity towards breast cancer cells that leave normal cells unaffected. These templates represent excellent scaffolds for the design of selective anticancer peptide therapeutics.