dbACP: A Comprehensive Database of Anti-Cancer Peptides

dbacp05130

General Description

Peptide name : Pal-pFL-N-Ter-TAT

Source/Organism : VDAC1(voltage-dependent anion channel1)

Linear/Cyclic : Linear

Chirality : L

Sequence Information

Sequence : FPWWWPFLRDVFTKGYGFGLGRKKRRQRRRPQ

Peptide length: 32

C-terminal modification: Linear

N-terminal modification : Not found

Non-natural peptide information: None

Activity Information

Assay type : MTT assay

Assay time : 4h

Activity : IC50 : 5.5 ± 1.1 μM

Cell line : A375

Cancer type : Leukemia

Other activity : Not found

Physicochemical Properties

Amino acid composition bar chart :

Molecular mass : 4123.7769 Dalton

Aliphatic index : 0.334

Instability index : 100.828

Hydrophobicity (GRAVY) : -1.306

Isoelectric point : 12

Charge (pH 7) : 8.7572

Aromaticity : 0.25

Molar extinction coefficient (cysteine, cystine): (17990, 17990)

Hydrophobic/hydrophilic ratio : 1.13333333

hydrophobic moment : 0.3744

Missing amino acid : C,H,M,I,E,S,N,A

Most occurring amino acid : R

Most occurring amino acid frequency : 7

Least occurring amino acid : D

Least occurring amino acid frequency : 1

Structural Information

3D structure :

Secondary structure fraction (Helix, Turn, Sheet): (0.1, 0.2, 0.3)

SMILES Notation: CC(C)C[C@H](NC(=O)CNC(=O)[C@H](Cc1ccccc1)NC(=O)CNC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H]1CCCN1C(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](N)Cc1ccccc1)C(C)C)[C@@H](C)O)C(=O)NCC(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(N)=O)C(=O)O

Secondary Structure :

Method Prediction
GOR CCCCCHHHHHHHETTCCCEHHHHHHHHHTCTT
Chou-Fasman (CF) EEEEECCEEEEEECEEEECHHHHHHHHCCCCC
Neural Network (NN) CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC
Joint/Consensus CCCCCCCCCCCCCCCCCCCHHHHHHHHCCCCC

Molecular Descriptors and ADMET Properties

Molecular Descriptors: Click here to download

ADMET Properties: Click here to download

Cross Referencing databases

Pubmed Id : 33757145

Uniprot : Not available

PDB : Not available

CancerPPD : Not available

ApIAPDB : Not available

CancerPPD2 ID : Not available

Reference

1 : Chatupheeraphat C, et al. A Novel Peptide Derived from Ginger Induces Apoptosis through the Modulation of p53, BAX, and BCL2 Expression in Leukemic Cell Lines. Planta Med. 2021; 87:560-569. doi: 10.1055/a-1408-5629

Literature

Paper title : A Novel Peptide Derived from Ginger Induces Apoptosis through the Modulation of p53, BAX, and BCL2 Expression in Leukemic Cell Lines.

Doi : https://doi.org/10.1055/a-1408-5629

Abstract : Despite the efficacy of chemotherapy, the adverse effects of chemotherapeutic drugs are considered a limitation of leukemia treatment. Therefore, a chemotherapy drug with minimal side effects is currently needed. One interesting molecule for this purpose is a bioactive peptide isolated from plants since it has less toxicity to normal cells. In this study, we extracted protein from the Zingiber officinale rhizome and performed purification to acquire the peptide fraction with the highest cytotoxicity using ultrafiltration, reverse-phase chromatography, and off-gel fractionation to get the peptide fraction that contained the highest cytotoxicity. Finally, a novel antileukemic peptide, P2 (sequence: RALGWSCL), was identified from the highest cytotoxicity fraction. The P2 peptide reduced the cell viability of NB4, MOLT4, and Raji cell lines without an effect on the normal peripheral blood mononuclear cells. The combination of P2 and daunorubicin significantly decreased leukemic cell viability when compared to treatment with either P2 or daunorubicin alone. In addition, leukemic cells treated with P2 demonstrated increased apoptosis and upregulation of caspase 3, 8, and 9 gene expression. Moreover, we also examined the effects of P2 on p53, which is the key regulator of apoptosis. Our results showed that treatment of leukemic cells with P2 led to the upregulation of p53 and Bcl-2-associated X protein, and the downregulation of B-cell lymphoma 2, indicating that p53 is involved in apoptosis induction by P2. The results of this study are anticipated to be useful for the development of P2 as an alternative drug for the treatment of leukemia.