dbACP: A Comprehensive Database of Anti-Cancer Peptides

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

Pubmed Id : 7628632 18957441

Uniprot : Not available

PDB : 1E4S

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.