dbACP: A Comprehensive Database of Anti-Cancer Peptides

dbacp03371

General Description

Peptide name : Ichthyophthirius multifiliis BP100

Source/Organism : White spot disease BP100

Linear/Cyclic : Not found

Chirality : Not found

Sequence Information

Sequence : KKLFKKILKYL

Peptide length: 11

C-terminal modification: Not found

N-terminal modification : Not found

Non-natural peptide information: None

Activity Information

Assay type : MTT assay

Assay time : Not found

Activity : MIC : 25 μM

Cell line : MCF-7

Cancer type : Breast cancer

Other activity : Not found

Physicochemical Properties

Amino acid composition bar chart :

Molecular mass : 1421.8542 Dalton

Aliphatic index : 1.418

Instability index : -10.218

Hydrophobicity (GRAVY) : -0.190

Isoelectric point : 10.301

Charge (pH 7) : 4.7541

Aromaticity : 0.181

Molar extinction coefficient (cysteine, cystine): (1490, 1490)

Hydrophobic/hydrophilic ratio : 0.83333333

hydrophobic moment : -0.253

Missing amino acid : C,R,W,H,Q,T,P,M,E,S,D,N,A,V,G

Most occurring amino acid : K

Most occurring amino acid frequency : 5

Least occurring amino acid : F

Least occurring amino acid frequency : 1

Structural Information

3D structure :

Secondary structure fraction (Helix, Turn, Sheet): (0.7, 0, 0.5)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CC(C)C)C(=O)O

Secondary Structure :

Method Prediction
GOR HHHHHHHHHHE
Chou-Fasman (CF) HHHHHHCCCCC
Neural Network (NN) HHHHHHHHHHH
Joint/Consensus HHHHHHHHHHC

Molecular Descriptors and ADMET Properties

Molecular Descriptors: Click here to download

ADMET Properties: Click here to download

Cross Referencing databases

Pubmed Id : 28524273

Uniprot : Not available

PDB : Not available

CancerPPD : Not available

ApIAPDB : Not available

CancerPPD2 ID : Not available

Reference

1 : Zhang B, et al. Synthesis and biological evaluation of novel peptides based on antimicrobial peptides as potential agents with antitumor and multidrug resistance-reversing activities. Chem Biol Drug Des. 2017; 90:972-980. doi: 10.1111/cbdd.13023

Literature

Paper title : Synthesis and biological evaluation of novel peptides based on antimicrobial peptides as potential agents with antitumor and multidrug resistance-reversing activities.

Doi : https://doi.org/10.1111/cbdd.13023

Abstract : Tumor chemotherapy, which plays an important role in the clinical treatment of metastatic cancer, is limited by low selectivity and drug resistance in clinical application. In our study, we selected antimicrobial peptide BP100 as a lead peptide, designed, and synthesized a series of novel antineoplastic peptides through solid-phase synthesis. Among them, B4 and B8 showed excellent anticancer activity. As revealed by further investigations, these peptides could disrupt the cell membrane, trigger the cytochrome C release into cytoplasm, and ultimately lead to apoptosis. In addition, they also showed multidrug resistance-reversing effects by performing effective antitumor activity against multidrug-resistant cells. As a result, these peptides may possibly be regarded as a promising candidate for cancer treatment.