dbacp05707
General Description
Peptide name : PTP-7b
Source/Organism : Synthetic peptide
Linear/Cyclic : Linear
Chirality : L
Sequence Information
Sequence : FLGALFKALSHLL
Peptide length: 13
C-terminal modification: Linear
N-terminal modification : Free
Non-natural peptide information: None
Activity Information
Assay type : MTT/MTS assay
Assay time : Not found
Activity : IC50 : 32 µM
Cell line : A-549
Cancer type : Lung cancer
Other activity : Anti-microbial activity
Physicochemical Properties
Amino acid composition bar chart :
Molecular mass : 1429.7469 Dalton
Aliphatic index : 1.653
Instability index : -8.8615
Hydrophobicity (GRAVY) : 1.5308
Isoelectric point : 8.7572
Charge (pH 7) : 0.8463
Aromaticity : 0.153
Molar extinction coefficient (cysteine, cystine): (0, 0)
Hydrophobic/hydrophilic ratio : 3.33333333
hydrophobic moment : 0.7999
Missing amino acid : C,R,W,Q,T,P,M,I,E,D,Y,N,V
Most occurring amino acid : L
Most occurring amino acid frequency : 5
Least occurring amino acid : G
Least occurring amino acid frequency : 1
Structural Information
3D structure :
Secondary structure fraction (Helix, Turn, Sheet): (0.6, 0.1, 0.5)
SMILES Notation: CC(C)C[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)Cc1ccccc1)C(=O)O
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | HHHHHHHHHHHHH |
| Chou-Fasman (CF) | HHHHHHHHHHCCC |
| Neural Network (NN) | HHHHHHHHHHHHH |
| Joint/Consensus | HHHHHHHHHHHHH |
Molecular Descriptors and ADMET Properties
Molecular Descriptors: Click here to download
ADMET Properties: Click here to download
Cross Referencing databases
Reference
1 : Chen L, et al. Peptide self-assembly on cell membranes to induce cell lysis. Biomacromolecules. 2012; 13:3327-33. doi: 10.1021/bm301106p
Literature
Paper title : Peptide self-assembly on cell membranes to induce cell lysis.
Doi : https://doi.org/10.1021/bm301106p
Abstract : Self-assembling into aggregates with defined structures is a common phenomenon for many peptides at high concentrations. In this study, we found that when PTP-7b (FLGALFKALSHLL), a concentration-dependent self-assembling peptide, bound to tissue cells and accumulated on cell surfaces, it migrated and self-assembled into exosome-like aggregates at certain locations on the cell membranes. Studies using confocal microscopy and scanning electron microscopy revealed that peptide PTP-7b induced cell tissue damage through a new cell lysis mechanism that involved peptide self-assembly on cell surfaces, extracting lipids from cell membranes, and transporting peptides into the cytoplasm. Peptide self-assembly attributed greatly to peptide-cell interactions and thus the biological activity of a peptide. Because peptide self-assembly was a slow process, PTP-7b-induced cell lysis showed a biphasic behavior: a gradual viability decrease was followed by a rapid decline. These results suggest that peptide self-assembly could be equally as important as charge and secondary structure of a peptide in determining the anticancer and antibacterial activities of therapeutic peptides.