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
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.