dbacp06321
General Description
Peptide name : TP
Source/Organism : Caecum-derived strain TS
Linear/Cyclic : Not found
Chirality : Not found
Sequence Information
Sequence : ASVVNKLTGGVAGLLK
Peptide length: 16
C-terminal modification: Not found
N-terminal modification : Free
Non-natural peptide information: None
Activity Information
Assay type : MTT assay
Assay time : 48h
Activity : IC 50: 11.479 μM
Cell line : NB4
Cancer type : Acute promyelocytic leukaemia
Other activity : Not found
Physicochemical Properties
Amino acid composition bar chart :
Molecular mass : 1526.8192 Dalton
Aliphatic index : 1.4
Instability index : 15.9687
Hydrophobicity (GRAVY) : 0.85
Isoelectric point : 10.003
Charge (pH 7) : 1.7939
Aromaticity : 0
Molar extinction coefficient (cysteine, cystine): (0, 0)
Hydrophobic/hydrophilic ratio : 2.2
hydrophobic moment : -0.072
Missing amino acid : C,R,W,H,Q,P,M,I,E,F,D,Y
Most occurring amino acid : V
Most occurring amino acid frequency : 3
Least occurring amino acid : S
Least occurring amino acid frequency : 1
Structural Information
3D structure :
Secondary structure fraction (Helix, Turn, Sheet): (0.4, 0.3, 0.4)
SMILES Notation: CC(C)C[C@H](NC(=O)CNC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)[C@H](C)N)C(C)C)C(C)C)[C@@H](C)O)C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)O
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | HEEEEEEETCEEEEEH |
| Chou-Fasman (CF) | EEECCEEEEEECCCCC |
| Neural Network (NN) | HHHHHCCCCCHHHHHH |
| Joint/Consensus | CEECCEEECCCCCCCC |
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 : Xin H, et al. Isolation and characterisation of a novel antibacterial peptide from a native swine intestinal tract-derived bacterium. Int J Antimicrob Agents. 2017; 49:427-436. doi: 10.1016/j.ijantimicag.2016.12.012
Literature
Paper title : Isolation and characterisation of a novel antibacterial peptide from a native swine intestinal tract-derived bacterium.
Doi : https://doi.org/10.1016/j.ijantimicag.2016.12.012
Abstract : Antimicrobial peptides (AMPs) are highly associated with antipathogenic activity, without generating drug resistance in targeted bacteria. In this study, the existence of AMPs in the Tibetan swine, a China-native, cold-resistant and seldom-sick breed of pig, was investigated. A peptide secreted by a Tibetan swine intestinal tract-derived Bacillus strain was isolated using reversed-phase chromatography (RPC), ultrafiltration and reversed-phase high-performance liquid chromatography (RP-HPLC). The peptide was identified by mass spectrometry and was characterised for activity against Escherichia coli and Staphylococcus aureus. The 16-amino acid peptide (ASVVNKLTGGVAGLLK), named TP, had a molecular mass of 1568.919 Da and exhibited inhibitory activity against Gram-positive and Gram-negative bacteria [minimum inhibitory concentrations (MICs) of 2.5-5 µM and 10-20 µM for E. coli and S. aureus, respectively] as well as human MKN-45 and NB4 tumour cell lines [50% inhibitory concentration (IC<sub>50</sub>) = 4.686 µM and 11.479 µM, respectively]. TP also exhibited weak haemolytic activity. Furthermore, TP enhanced cell membrane permeability and K+ outflow, bound with E. coli genomic DNA in vitro and inhibited E. coli growth. Thus, TP represents a strong candidate as an antibacterial peptide.