dbACP: A Comprehensive Database of Anti-Cancer Peptides

dbacp06030

General Description

Peptide name : SCH-P9

Source/Organism : Marine invertebrates

Linear/Cyclic : Linear

Chirality : L

Sequence Information

Sequence : LPGP

Peptide length: 4

C-terminal modification: Linear

N-terminal modification : Not found

Non-natural peptide information: None

Activity Information

Assay type : MTT assay

Assay time : 24h

Activity : IC50 : 1.09 mg/mL

Cell line : PC-3

Cancer type : Prostate cancer

Other activity : Not found

Physicochemical Properties

Amino acid composition bar chart :

Molecular mass : 382.4546 Dalton

Aliphatic index : 0.975

Instability index : 55.65

Hydrophobicity (GRAVY) : 0.05

Isoelectric point : 5.525

Charge (pH 7) : -0.2399

Aromaticity : 0

Molar extinction coefficient (cysteine, cystine): (0, 0)

Hydrophobic/hydrophilic ratio : infinite

hydrophobic moment : 0.9134

Missing amino acid : W,T,I,M,E,K,F,D,N,C,R,H,Q,S,Y,A,V

Most occurring amino acid : P

Most occurring amino acid frequency : 2

Least occurring amino acid : L

Least occurring amino acid frequency : 1

Structural Information

3D structure :

Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.7, 0.2)

SMILES Notation: CC(C)C[C@H](N)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N1CCC[C@H]1C(=O)O

Secondary Structure :

Method Prediction
GOR CCCC
Chou-Fasman (CF) CCCC
Neural Network (NN) CCCC
Joint/Consensus CCCC

Molecular Descriptors and ADMET Properties

Molecular Descriptors: Click here to download

ADMET Properties: Click here to download

Cross Referencing databases

Pubmed Id : 28901516

Uniprot : Not available

PDB : Not available

CancerPPD : Not available

ApIAPDB : Not available

CancerPPD2 ID : Not available

Reference

1 : Huang F, et al. Two novel peptides derived from Sinonovacula constricta inhibit the proliferation and induce apoptosis of human prostate cancer cells. Mol Med Rep. 2017; 16:6697-6707. doi: 10.3892/mmr.2017.7418

Literature

Paper title : Two novel peptides derived from Sinonovacula constricta inhibit the proliferation and induce apoptosis of human prostate cancer cells.

Doi : https://doi.org/10.3892/mmr.2017.7418

Abstract : In China, the incidence of prostate cancer has been increasing. Toxicity, drug resistance and limited transient benefits in patients are the main problems associated with standard chemotherapeutic regimens, and new drugs are therefore required to treat prostate cancer. SCH‑P9 and SCH‑P10 proteins were obtained from Sinonovacula constricta hydrolysates. The amino acid sequences of SCH‑P9 and SCH‑P10 were identified as Leu‑Pro‑Gly‑Pro and Asp‑Tyr‑Val‑Pro, with molecular weights of 382.46 Da and 492.53 Da, respectively. An MTT assay, annexin V‑fluorescein isothiocyanate (FITC) staining and cell cycle analysis were applied to identify the viability of cells, stages of apoptosis, and cell cycle distribution, respectively. SCH‑P9 and SCH‑P10 inhibited the growth of DU‑145 and PC‑3 cells in a dose‑ and time‑dependent manner. Annexin V‑FITC staining and flow cytometry analysis were employed to measure apoptosis and cell cycle arrest, respectively. SCH‑P9 and SCH‑P10 inhibited the growth of DU‑145 cells by reducing the number of cells in G0/G1 phase, increasing the number in subG1 phase and inducing apoptosis. SCH‑P9 reduced the number of PC‑3 cells in subG1 and G0/G1 phases, increased the number of cells in G2/M phase and induced apoptosis. SCH‑P10 reduced the number of PC‑3 cells in G2/M phase, increased the number of cells in G0/G1 phase and induced apoptosis. In conclusion, the results demonstrated that SCH‑P9 and SCH‑P10 induced apoptosis in DU‑145 and PC‑3 cells and may, therefore, exhibit potential for application in the treatment of prostate cancer.