dbACP: A Comprehensive Database of Anti-Cancer Peptides

dbacp06522

General Description

Peptide name : Viscotoxin A3

Source/Organism : The European mistletoe

Linear/Cyclic : Not found

Chirality : L

Sequence Information

Sequence : KSCCPNTTGRNIYNACRLTGAPRPTCAKLSGCKIISGSTCPSDYPK

Peptide length: 46

C-terminal modification: Not found

N-terminal modification : Free

Non-natural peptide information: None

Activity Information

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Not found

Cancer type : Breast cancer

Other activity : Anti-microbial activity

Physicochemical Properties

Amino acid composition bar chart :

Molecular mass : 4835.5695 Dalton

Aliphatic index : 0.489

Instability index : 49.5609

Hydrophobicity (GRAVY) : -0.463

Isoelectric point : 9.3029

Charge (pH 7) : 5.6958

Aromaticity : 0.043

Molar extinction coefficient (cysteine, cystine): (2980, 3355)

Hydrophobic/hydrophilic ratio : 1

hydrophobic moment : 0.304

Missing amino acid : W,H,Q,M,E,F,V

Most occurring amino acid : C

Most occurring amino acid frequency : 6

Least occurring amino acid : D

Least occurring amino acid frequency : 1

Structural Information

3D structure :

Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.3, 0.2)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CS)NC(=O)[C@H](CS)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CCCCN)[C@@H](C)O)[C@@H](C)O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCNC(=N)N)C(=O)N1CCC[C@H]1C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CS)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCCN)C(=O)O)[C@@H](C)O)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)[C@@H](C)O

Secondary Structure :

Method Prediction
GOR TTTCTTTCCCEEEETEEETTCCCCCCTTTTTEEEEETCCCCCCCCT
Chou-Fasman (CF) CCCCCEECEEEECCCEEECCCCCCCCCCCCEEEEEEECCCCCCCCC
Neural Network (NN) CCCCCCCCCCCEEEEECCCCCCCCCCCCCCCCEEEECCCCCCCCCC
Joint/Consensus CCCCCCCCCCEEEEEEEECCCCCCCCCCCCCEEEEECCCCCCCCCC

Molecular Descriptors and ADMET Properties

Molecular Descriptors: Click here to download

ADMET Properties: Click here to download

Cross Referencing databases

Pubmed Id : 5719166 18957441

Uniprot : Not available

PDB : 1ED0

CancerPPD : Not available

ApIAPDB : Not available

CancerPPD2 ID : Not available

Reference

1 : Samuelsson G, et al. The amino acid sequence of oxidized viscotoxin A3 from the European mistletoe (Viscum album L, Loranthaceae). Acta Chem Scand. 1968; 22:2624-42. doi: 10.3891/acta.chem.scand.22-2624

2 : Wang G, et al. APD2: the updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res. 2009; 37:D933-7. doi: 10.1093/nar/gkn823

Literature

Paper title : The amino acid sequence of oxidized viscotoxin A3 from the European mistletoe (Viscum album L, Loranthaceae).

Doi : https://doi.org/10.3891/acta.chem.scand.22-2624

Abstract : Not available

Paper title : APD2: the updated antimicrobial peptide database and its application in peptide design.

Doi : https://doi.org/10.1093/nar/gkn823

Abstract : The antimicrobial peptide database (APD, http://aps.unmc.edu/AP/main.php) has been updated and expanded. It now hosts 1228 entries with 65 anticancer, 76 antiviral (53 anti-HIV), 327 antifungal and 944 antibacterial peptides. The second version of our database (APD2) allows users to search peptide families (e.g. bacteriocins, cyclotides, or defensins), peptide sources (e.g. fish, frogs or chicken), post-translationally modified peptides (e.g. amidation, oxidation, lipidation, glycosylation or d-amino acids), and peptide binding targets (e.g. membranes, proteins, DNA/RNA, LPS or sugars). Statistical analyses reveal that the frequently used amino acid residues (>10%) are Ala and Gly in bacterial peptides, Cys and Gly in plant peptides, Ala, Gly and Lys in insect peptides, and Leu, Ala, Gly and Lys in amphibian peptides. Using frequently occurring residues, we demonstrate database-aided peptide design in different ways. Among the three peptides designed, GLK-19 showed a higher activity against Escherichia coli than human LL-37.