dbacp03322
General Description
Peptide name : hP4
Source/Organism : Human endostatin peptides
Linear/Cyclic : Linear
Chirality : L
Sequence Information
Sequence : AAVPIVNLKDELLFPSWEALFSGSE
Peptide length: 25
C-terminal modification: Linear
N-terminal modification : Free
Non-natural peptide information: None
Activity Information
Assay type : Matrigel assay
Assay time : 72h
Activity : No inhibition at 7 mg/kg/d
Cell line : BxPC-3
Cancer type : Pancreatic cancer
Other activity : Not found
Physicochemical Properties
Amino acid composition bar chart :
Molecular mass : 2733.0744 Dalton
Aliphatic index : 1.132
Instability index : 33.624
Hydrophobicity (GRAVY) : 0.432
Isoelectric point : 4.2445
Charge (pH 7) : -3.1903
Aromaticity : 0.12
Molar extinction coefficient (cysteine, cystine): (5500, 5500)
Hydrophobic/hydrophilic ratio : 1.77777777
hydrophobic moment : 0.161
Missing amino acid : C,R,H,Q,T,M,Y
Most occurring amino acid : L
Most occurring amino acid frequency : 4
Least occurring amino acid : I
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@H](C)[C@H](NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](C)N)C(C)C)C(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1ccccc1)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(=O)O)C(=O)O)C(C)C
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | HHCHHHHCTHHHHCHHHHHHHTTCH |
| Chou-Fasman (CF) | CEEEEHHHHHHHCCCHHHHCCCCCC |
| Neural Network (NN) | CCCHHHHCCCCHCCCCCHHHCCCCC |
| Joint/Consensus | CCCHHHHCCCCCCCCHHHHHCCCCC |
Molecular Descriptors and ADMET Properties
Molecular Descriptors: Click here to download
ADMET Properties: Click here to download
Cross Referencing databases
Reference
1 : Tjin Tham Sjin RM, et al. A 27-amino-acid synthetic peptide corresponding to the NH2-terminal zinc-binding domain of endostatin is responsible for its antitumor activity. Cancer Res. 2005; 65:3656-63. doi: 10.1158/0008-5472.CAN-04-1833
Literature
Paper title : A 27-amino-acid synthetic peptide corresponding to the NH2-terminal zinc-binding domain of endostatin is responsible for its antitumor activity.
Doi : https://doi.org/10.1158/0008-5472.CAN-04-1833
Abstract : The first recombinant endostatin that elicited strong antitumor activity was expressed in Escherichia coli and administered as a suspension. Under these conditions, the protein retained its full antiangiogenic activity. Lack of requirement for a folded structure prompted us to investigate antitumor properties of synthetic peptides corresponding to different regions of endostatin. Here, we show that the entire antitumor, antimigration, and antipermeability activities of endostatin are mimicked by a 27-amino-acid peptide corresponding to the NH2-terminal domain of endostatin. This peptide contains three histidines that are responsible for zinc binding. Mutations of the zinc-binding histidines abolished its antitumor and antimigration activities, but not antipermeability properties.