dbACP: A Comprehensive Database of Anti-Cancer Peptides

dbacp04343

General Description

Peptide name : Lycosin-I

Source/Organism : Venom, wolf spider

Linear/Cyclic : Not found

Chirality : Not found

Sequence Information

Sequence : RKGWFKAMKSIAKFIAKEKLKEHL-OH

Peptide length: Not available

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 : Not found

Other activity : Not found

Physicochemical Properties

Amino Acid Composition Bar Chart : Not available

Molecular mass : Not available

Aliphatic index : Not available

Instability index : Not available

Hydrophobicity (GRAVY) : Not available

Isoelectric point : Not available

Charge (pH 7) : Not available

Aromaticity : Not available

Molar extinction coefficient (cysteine, cystine): Not available

Hydrophobic/hydrophilic ratio : Not available

hydrophobic moment : Not available

Missing amino acid : Not available

Most occurring amino acid : Not available

Most occurring amino acid frequency : Not available

Least occurring amino acid : Not available

Least occurring amino acid frequency : Not available

Structural Information

3D-structure: Not available

Secondary structure fraction (Helix, Turn, Sheet): Not available

SMILES Notation: Not available

Secondary Structure :

Method Prediction
GOR Not available
Chou-Fasman (CF) Not available
Neural Network (NN) Not available
Joint/Consensus Not available

Molecular Descriptors and ADMET Properties

Molecular descriptors: Not available

ADMET properties: Not available

Cross Referencing Databases databases

Pubmed Id : 22882120, .

Uniprot : Click here

CancerPPD : Not available

ApIAPDB : Not available

Reference

1 : Liu Z, et al. A novel spider peptide toxin suppresses tumor growth through dual signaling pathways. Curr Mol Med. 2012; 12:1350-60. doi: 10.2174/156652412803833643

Literature

Paper title : A novel spider peptide toxin suppresses tumor growth through dual signaling pathways.

Doi : https://doi.org/10.2174/156652412803833643

Abstract : Spider venom is a large pharmacological repertoire containing many biologically active peptides, which may have a potent therapeutic implication. Here we investigated a peptide toxin, named lycosin-I, isolated from the venom of the spider Lycosa singoriensis. In contrast to most spider peptide toxins adopting inhibitor cystine knot (ICK) motif, lycosin-I shows a linear amphipathic alpha-helical conformation, common to α-helical host defense peptides. Lycosin-I displays strong ability to inhibit cancer cell growth in vitro and can effectively suppresses tumor growth in vivo. Mechanistically, it activates the mitochondrial death pathway to sensitize cancer cells for apoptosis, as well as up-regulates p27 to inhibit cell proliferation. Taken together, our results provide the first evidence that a spider toxin can effectively suppress tumorigenesis through activation of dual signaling pathways. In addition, lycosin-I may be a useful structural lead for the development of novel anticancer drugs.