dbACP: A Comprehensive Database of Anti-Cancer Peptides

dbacp03333

General Description

Peptide name : Human beta defensin 3

Source/Organism : Skin, tonsils, oral/saliva, colonic mucosa, Human

Linear/Cyclic : Not found

Chirality : Not found

Sequence Information

Sequence : GIINTLQKYYCRVRGGRCAVLSCLPKEEQIGKCSTRGRKCCRRKK

Peptide length: 45

C-terminal modification: Not found

N-terminal modification : Not found

Non-natural peptide information: None

Activity Information

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Not found

Cancer type : Not found

Other activity : Anti- microbial activity

Physicochemical Properties

Amino acid composition bar chart :

Molecular mass : 5161.1614 Dalton

Aliphatic index : 0.671

Instability index : 53.1311

Hydrophobicity (GRAVY) : -0.7

Isoelectric point : 10.082

Charge (pH 7) : 10.6983

Aromaticity : 0.044

Molar extinction coefficient (cysteine, cystine): (2980, 3355)

Hydrophobic/hydrophilic ratio : 0.875

hydrophobic moment : 0.0856

Missing amino acid : W,H,M,F,D

Most occurring amino acid : R

Most occurring amino acid frequency : 7

Least occurring amino acid : N

Least occurring amino acid frequency : 1

Structural Information

3D structure :

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

SMILES Notation: CC[C@H](C)[C@H](NC(=O)CN)C(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@H](C(=O)N[C@@H](CCCNC(=N)N)C(=O)NCC(=O)NCC(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CS)C(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@@H](CCCNC(=N)N)C(=O)NCC(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)O)[C@@H](C)O)[C@@H](C)CC)C(C)C)C(C)C)[C@@H](C)O)[C@@H](C)CC

Secondary Structure :

Method Prediction
GOR EEECCCTTEEEEETTCCEEEETTCCTHHHHTTCCCTTTHHHHTTT
Chou-Fasman (CF) EEEECCEEEEEEECCCEEEEECHHHHHHEECEEEECCCCCCCCCC
Neural Network (NN) CCEECCCCEEEEECCCCEEECCCCCCCCCCCCCCCCCCCCCCCCC
Joint/Consensus EEEECCCCEEEEECCCCEEEECCCCCCCCCCCCCCCCCCCCCCCC

Molecular Descriptors and ADMET Properties

Molecular Descriptors: Click here to download

ADMET Properties: Click here to download

Cross Referencing databases

Pubmed Id : 11085990

Uniprot : Not available

PDB : 1KJ6

CancerPPD : Not available

ApIAPDB : Not available

CancerPPD2 ID : Not available

Reference

1 : Harder J, et al. Isolation and characterization of human beta -defensin-3, a novel human inducible peptide antibiotic. J Biol Chem. 2001; 276:5707-13. doi: 10.1074/jbc.M008557200

Literature

Paper title : Isolation and characterization of human beta -defensin-3, a novel human inducible peptide antibiotic.

Doi : https://doi.org/10.1074/jbc.M008557200

Abstract : The growing public health problem of infections caused by multiresistant Gram-positive bacteria, in particular Staphylococcus aureus, prompted us to screen human epithelia for endogenous S. aureus-killing factors. A novel 5-kDa, nonhemolytic antimicrobial peptide (human beta-defensin-3, hBD-3) was isolated from human lesional psoriatic scales and cloned from keratinocytes. hBD-3 demonstrated a salt-insensitive broad spectrum of potent antimicrobial activity against many potentially pathogenic microbes including multiresistant S. aureus and vancomycin-resistant Enterococcus faecium. Ultrastructural analyses of hBD-3-treated S. aureus revealed signs of cell wall perforation. Recombinant hBD-3 (expressed as a His-Tag-fusion protein in Escherichia coli) and chemically synthesized hBD-3 were indistinguishable from naturally occurring peptide with respect to their antimicrobial activity and biochemical properties. Investigation of different tissues revealed skin and tonsils to be major hBD-3 mRNA-expressing tissues. Molecular cloning and biochemical analyses of antimicrobial peptides in cell culture supernatants revealed keratinocytes and airway epithelial cells as cellular sources of hBD-3. Tumor necrosis factor alpha and contact with bacteria were found to induce hBD-3 mRNA expression. hBD-3 therefore might be important in the innate epithelial defense of infections by various microorganisms seen in skin and lung, such as cystic fibrosis.