dbACP: A Comprehensive Database of Anti-Cancer Peptides

dbacp04311

General Description

Peptide name : Lunasin

Source/Organism : Soyabean

Linear/Cyclic : Not found

Chirality : Not found

Sequence Information

Sequence : SKWQHQQDSCRKQLQGVNLTPCEKHIMEKIQGRGDDDDDDDDD

Peptide length: 43

C-terminal modification: Not found

N-terminal modification : Free

Non-natural peptide information: None

Activity Information

Assay type : TUNEL DNA fragmentation assay

Assay time : 48h

Activity : Not found

Cell line : MCF-7

Cancer type : Breast cancer

Other activity : Not found

Physicochemical Properties

Amino acid composition bar chart :

Molecular mass : 5028.315 Dalton

Aliphatic index : 0.430

Instability index : 48.3814

Hydrophobicity (GRAVY) : -1.762

Isoelectric point : 4.5035

Charge (pH 7) : -6.3693

Aromaticity : 0.023

Molar extinction coefficient (cysteine, cystine): (5500, 5625)

Hydrophobic/hydrophilic ratio : 0.43333333

hydrophobic moment : 0.1417

Missing amino acid : A,F,Y

Most occurring amino acid : D

Most occurring amino acid frequency : 10

Least occurring amino acid : W

Least occurring amino acid frequency : 1

Structural Information

3D structure :

Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.4, 0.1)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCSC)NC(=O)[C@@H](NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CS)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CS)NC(=O)[C@H](CO)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CO)C(C)C)[C@@H](C)O)[C@@H](C)CC)C(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CCCNC(=N)N)C(=O)NCC(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)O

Secondary Structure :

Method Prediction
GOR HHHHHTTHHHHHTETCCTCCHHHHHHHHHHHCCCCCCCCCCTT
Chou-Fasman (CF) HHHHHHCCCHHHHEEEECCCHHHHHHHHEECCCCHHHHHHCCC
Neural Network (NN) CCCCCCCCCCCCCCCCCCCCCCCCCHHHHCCCCCCCCCCCCCC
Joint/Consensus HHHHHCCCCCCCCCCCCCCCHHHHHHHHHCCCCCCCCCCCCCC

Molecular Descriptors and ADMET Properties

Molecular Descriptors: Click here to download

ADMET Properties: Click here to download

Cross Referencing databases

Pubmed Id : 10331812

Uniprot : Not available

PDB : Not available

CancerPPD : Not available

ApIAPDB : Not available

CancerPPD2 ID : Not available

Reference

1 : Galvez AF and de Lumen BO. A soybean cDNA encoding a chromatin-binding peptide inhibits mitosis of mammalian cells. Nat Biotechnol. 1999; 17:495-500. doi: 10.1038/8676

Literature

Paper title : A soybean cDNA encoding a chromatin-binding peptide inhibits mitosis of mammalian cells.

Doi : https://doi.org/10.1038/8676

Abstract : A soybean cDNA encoding the small subunit peptide of a cotyledon-specific 2S albumin (Gm2S-1) is thought to play a role in arresting mitosis during the DNA endoreduplication and cell expansion phase of seed development. The peptide (termed lunasin) contains the cell adhesion motif Arg-Gly-Asp (RGD) followed by eight aspartic acid residues at its C-terminal end. A chimeric gene encoding the lunasin peptide tagged with green fluorescent protein (GFP) arrested cell division, caused abnormal spindle fiber elongation, chromosomal fragmentation, and cell lysis when transiently transfected into murine embryo fibroblast, murine hepatoma, and human breast cancer cells. Deletion of the polyaspartyl end abolished the antimitotic effect. Subcellular localization of lunasin and immunobinding assay using synthetic peptides revealed the preferential adherence of lunasin to chromatin. Immunofluorescence showed that kinetochore proteins were displaced from the centromere in lunasin-transfected cells. These observations suggest that lunasin binds to the chromatin, leading to disruption of kinetochore formation and inhibition of mitosis.