dbACP: A Comprehensive Database of Anti-Cancer Peptides

dbacp04320

General Description

Peptide name : LvHemB1

Source/Organism : Marine invertebrates

Linear/Cyclic : Linear

Chirality : L

Sequence Information

Sequence : DVNFLLHKIYGNIRY

Peptide length: 15

C-terminal modification: Linear

N-terminal modification : Not found

Non-natural peptide information: None

Activity Information

Assay type : MTT assay

Assay time : 24h

Activity : Not found

Cell line : HeLa

Cancer type : Bladder cancer

Other activity : Not found

Physicochemical Properties

Amino acid composition bar chart :

Molecular mass : 1865.1381 Dalton

Aliphatic index : 1.233

Instability index : 22.3867

Hydrophobicity (GRAVY) : -0.1

Isoelectric point : 8.5042

Charge (pH 7) : 0.8454

Aromaticity : 0.2

Molar extinction coefficient (cysteine, cystine): (2980, 2980)

Hydrophobic/hydrophilic ratio : 0.875

hydrophobic moment : -0.178

Missing amino acid : C,W,Q,T,P,M,E,S,A

Most occurring amino acid : N

Most occurring amino acid frequency : 2

Least occurring amino acid : D

Least occurring amino acid frequency : 1

Structural Information

3D structure :

Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.2, 0.5)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC(=O)O)C(C)C)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)O)[C@@H](C)CC

Secondary Structure :

Method Prediction
GOR HHHHHHHEETTCEEE
Chou-Fasman (CF) EEHHHHEEEEEECCC
Neural Network (NN) HHHHHHHHCCCCCEE
Joint/Consensus HHHHHHHEECCCCEE

Molecular Descriptors and ADMET Properties

Molecular Descriptors: Click here to download

ADMET Properties: Click here to download

Cross Referencing databases

Pubmed Id : 33630204

Uniprot : Not available

PDB : Not available

CancerPPD : Not available

ApIAPDB : Not available

CancerPPD2 ID : Not available

Reference

1 : Liu S, et al. LvHemB1, a novel cationic antimicrobial peptide derived from the hemocyanin of Litopenaeus vannamei, induces cancer cell death by targeting mitochondrial voltage-dependent anion channel 1. Cell Biol Toxicol. 2022; 38:87-110. doi: 10.1007/s10565-021-09588-y

Literature

Paper title : LvHemB1, a novel cationic antimicrobial peptide derived from the hemocyanin of Litopenaeus vannamei, induces cancer cell death by targeting mitochondrial voltage-dependent anion channel 1.

Doi : https://doi.org/10.1007/s10565-021-09588-y

Abstract : Current cancer treatment regimens such as chemotherapy and traditional chemical drugs have adverse side effects including the appearance of drug-resistant tumor cells. For these reasons, it is imperative to find novel therapeutic agents that overcome these factors. To this end, we explored a cationic antimicrobial peptide derived from Litopenaeus vannamei hemocyanin (designated LvHemB1) that induces cancer cell death, but sparing normal cells. LvHemB1 inhibits the proliferation of human cervical (HeLa), esophageal (EC109), hepatocellular (HepG2), and bladder (EJ) cancer cell lines, but had no significant effect on normal liver cell lines (T-antigen-immortalized human liver epithelial (THLE-3) cells). In addition to its antiproliferative effects, LvHemB1 induced apoptosis, by permeating cells and targeting mitochondrial voltage-dependent anion channel 1 (VDAC1). Colocalization studies revealed the localization of LvHemB1 in mitochondria, while molecular docking and pull-down analyses confirmed LvHemB1-VDAC1 interaction. Moreover, LvHemB1 causes loss in mitochondrial membrane potential and increases levels of reactive oxygen species (ROS) and apoptotic proteins (caspase-9, caspase-3, and Bax (Bcl-2-associated X)), which results in mitochondrial-mediated apoptosis. Thus, peptide LvHemB1 has the potential of being used as an anticancer agent due to its antiproliferation effect and targeting to VDAC1 to cause mitochondrial dysfunction in cancer cells, as well as its ability to induce apoptosis by increasing ROS levels, and the expression of proapoptotic proteins.