dbACP: A Comprehensive Database of Anti-Cancer Peptides

dbacp06526

General Description

Peptide name : Viscotoxin B2

Source/Organism : Korean mistletoe

Linear/Cyclic : Not found

Chirality : L

Sequence Information

Sequence : KSCCKNTTGRNIYNTCRFAGGSRERCAKLSGCKIISASTCPSDYPK

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 : 4977.6855 Dalton

Aliphatic index : 0.404

Instability index : 37.8022

Hydrophobicity (GRAVY) : -0.641

Isoelectric point : 9.4559

Charge (pH 7) : 6.6976

Aromaticity : 0.065

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

Hydrophobic/hydrophilic ratio : 0.76923076

hydrophobic moment : 0.4566

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

Most occurring amino acid : S

Most occurring amino acid frequency : 6

Least occurring amino acid : F

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](CCCCN)NC(=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(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](C)C(=O)NCC(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCNC(=N)N)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)N[C@@H](C)C(=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

Secondary Structure :

Method Prediction
GOR TTTTTTTTCCCCEEEEEETTTCHHHHHTTTTCEEEEETCCCTCCCT
Chou-Fasman (CF) CCCCEEECEEEEEEECCCCCCHHHHHHCCCEEEEEEECCCCCCCCC
Neural Network (NN) CCCCCCCCCCEEEEEEECCCCCCHHHHHCCCCEEEECCCCCCCCCC
Joint/Consensus CCCCCCCCCCEEEEEEECCCCCHHHHHCCCCCEEEEECCCCCCCCC

Molecular Descriptors and ADMET Properties

Molecular Descriptors: Click here to download

ADMET Properties: Click here to download

Cross Referencing databases

Pubmed Id : 15700822 18957441

Uniprot : Not available

PDB : Not available

CancerPPD : Not available

ApIAPDB : Not available

CancerPPD2 ID : Not available

Reference

1 : 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

2 : Kong JL, et al. [Determination of primary structure of a novel peptide from mistletoe and its antitumor activity]. Yao Xue Xue Bao. 2004; 39:813-7.

Literature

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.

Paper title : [Determination of primary structure of a novel peptide from mistletoe and its antitumor activity].

Doi : https://doi.org/Not available

Abstract : AIM: To study the antitumor peptide components in the stems and leaves of mistletoe (Viscum coloratum (Kom.) Nakai), the primary structure of the novel peptide was elucidated. METHODS: Cation exchange, gel filtration and HPLC were employed for isolation and purification. Matrix Assisted Laser Desorption Ionization-Time of Flight-Mass Spectrometry was used to determine the mass. The complete amino acid sequence of the novel peptide was obtained by Edman degradation combined with enzyme digestion. The antitumor activity of the peptide in vitro was studied with MTT method. RESULTS: The primary stucture of the peptide named as viscotoxin B2 is KSCCKNTTGRNIYNTCRFAGGSRERCAKLSGCKIISASTCPSDYPK. The IC50 value of viscotoxin B2 on the Rat Osteoblast-like Sarcoma 17/2.8 cells in vitro is 1.6 mg x L(-1). CONCLUSION: Viscotoxin B2 in V. coloratum, which has high similarity with viscotoxins from V. album, showed antitumor activity.