dbacp03281
General Description
Peptide name : hBD-1
Source/Organism : Keratinocytes; skin; platelets; Human
Linear/Cyclic : Not found
Chirality : L
Sequence Information
Sequence : DHYNCVSSGGQCLYSACPIFTKIQGTCYRGKAKCCK
Peptide length: 36
C-terminal modification: Not found
N-terminal modification : Free
Non-natural peptide information: None
Activity Information
Assay type : Not specified
Assay time : Not found
Activity : Not found
Cell line : Not found
Cancer type : Fibrosarcoma
Other activity : Anti-microbial activity
Physicochemical Properties
Amino acid composition bar chart :
Molecular mass : 3934.5484 Dalton
Aliphatic index : 0.461
Instability index : 34.4917
Hydrophobicity (GRAVY) : -0.272
Isoelectric point : 8.8709
Charge (pH 7) : 3.782
Aromaticity : 0.111
Molar extinction coefficient (cysteine, cystine): (4470, 4845)
Hydrophobic/hydrophilic ratio : 1
hydrophobic moment : 0.0108
Missing amino acid : W,M,E
Most occurring amino acid : C
Most occurring amino acid frequency : 6
Least occurring amino acid : D
Least occurring amino acid frequency : 1
Structural Information
3D structure :
Secondary structure fraction (Helix, Turn, Sheet): (0.1, 0.2, 0.2)
SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](NC(=O)[C@@H]1CCCN1C(=O)[C@H](CS)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CCC(N)=O)NC(=O)CNC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CS)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@@H](N)CC(=O)O)C(C)C)[C@@H](C)CC)[C@@H](C)O)C(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCCNC(=N)N)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCCN)C(=O)O)[C@@H](C)O
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | TCEEEEETTCCEEETTCCEEEEETTCCCTTTTTHHT |
| Chou-Fasman (CF) | CCEEEECCCEEEEECEEEEEEEEEEEECHHHHHCCC |
| Neural Network (NN) | CCCCCCCCCCCEECCCCCCCEECCCCCCCCCCCCCC |
| Joint/Consensus | CCEEEECCCCCEEECCCCEEEEECCCCCCCCCCCCC |
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 : Bensch KW, et al. hBD-1: a novel beta-defensin from human plasma. FEBS Lett. 1995; 368:331-5. doi: 10.1016/0014-5793(95)00687-5
2 : Wang G, et al. APD2: the updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res. 2009; 37:D933-7. doi: 10.1093/nar/gkn823
Literature
Paper title : hBD-1: a novel beta-defensin from human plasma.
Doi : https://doi.org/10.1016/0014-5793(95)00687-5
Abstract : We report the isolation and characterization of a novel peptide with significant sequence homology to beta-defensins from human blood filtrate. The human beta-defensin-1 (hBD-1) is a short basic peptide of 36 amino acid residues. It contains six cysteines forming three intramolecular disulfide bonds. The molecular mass of hBD-1 is 3928.6 Da. Cloning of the specific cDNA confirmed the amino acid sequence of the native peptide. hBD-1 shares the nine conserved amino acids characteristic for beta-defensins from respiratory epithelial cells and neutrophils of cattle and chicken leukocytes. hBD-1 is present in nanomolar concentration in human plasma.
Paper title : APD2: the updated antimicrobial peptide database and its application in peptide design.
Doi : https://doi.org/10.1093/nar/gkn823
Abstract : The antimicrobial peptide database (APD, http://aps.unmc.edu/AP/main.php) has been updated and expanded. It now hosts 1228 entries with 65 anticancer, 76 antiviral (53 anti-HIV), 327 antifungal and 944 antibacterial peptides. The second version of our database (APD2) allows users to search peptide families (e.g. bacteriocins, cyclotides, or defensins), peptide sources (e.g. fish, frogs or chicken), post-translationally modified peptides (e.g. amidation, oxidation, lipidation, glycosylation or d-amino acids), and peptide binding targets (e.g. membranes, proteins, DNA/RNA, LPS or sugars). Statistical analyses reveal that the frequently used amino acid residues (>10%) are Ala and Gly in bacterial peptides, Cys and Gly in plant peptides, Ala, Gly and Lys in insect peptides, and Leu, Ala, Gly and Lys in amphibian peptides. Using frequently occurring residues, we demonstrate database-aided peptide design in different ways. Among the three peptides designed, GLK-19 showed a higher activity against Escherichia coli than human LL-37.