dbACP: A Comprehensive Database of Anti-Cancer Peptides

dbacp02665

General Description

Peptide name : Dermaseptin-L1 (DRS-L1)

Source/Organism : Lemur leaf frog

Linear/Cyclic : Not found

Chirality : L

Sequence Information

Sequence : GLWSKIKEAAKAAGKAALNAVTGLVNQGDQPS

Peptide length: 32

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 : Colorectal cancer

Other activity : Anti-bacterial activity; Anti-microbial activity

Physicochemical Properties

Amino acid composition bar chart :

Molecular mass : 3194.596 Dalton

Aliphatic index : 0.887

Instability index : 13.5031

Hydrophobicity (GRAVY) : -0.190

Isoelectric point : 9.5282

Charge (pH 7) : 1.76

Aromaticity : 0.031

Molar extinction coefficient (cysteine, cystine): (5500, 5500)

Hydrophobic/hydrophilic ratio : 1.46153846

hydrophobic moment : -1.040

Missing amino acid : C,R,H,M,F,Y

Most occurring amino acid : A

Most occurring amino acid frequency : 7

Least occurring amino acid : W

Least occurring amino acid frequency : 1

Structural Information

3D structure :

Secondary structure fraction (Helix, Turn, Sheet): (0.4, 0.3, 0.2)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CC(C)C)NC(=O)CN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCC(N)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)O)C(C)C)[C@@H](C)O)C(C)C

Secondary Structure :

Method Prediction
GOR THHHHHHHHHHHHHHHHHHHEEEEEECCCCCC
Chou-Fasman (CF) CCCHHHHHHHHHHHHHHHEEEEEEECCCCCCC
Neural Network (NN) CCCHHHHHHHHHHHHHHHHHHHCCCCCCCCCC
Joint/Consensus CCCHHHHHHHHHHHHHHHHHEEEEECCCCCCC

Molecular Descriptors and ADMET Properties

Molecular Descriptors: Click here to download

ADMET Properties: Click here to download

Cross Referencing databases

Pubmed Id : 17561225 18644413

Uniprot : Not available

PDB : Not available

CancerPPD : Not available

ApIAPDB : Not available

CancerPPD2 ID : Not available

Reference

1 : Amiche M, et al. A consistent nomenclature of antimicrobial peptides isolated from frogs of the subfamily Phyllomedusinae. Peptides. 2008; 29:2074-82. doi: 10.1016/j.peptides.2008.06.017

2 : Conlon JM, et al. Peptides with differential cytolytic activity from skin secretions of the lemur leaf frog Hylomantis lemur (Hylidae: Phyllomedusinae). Toxicon. 2007; 50:498-506. doi: 10.1016/j.toxicon.2007.04.017

Literature

Paper title : A consistent nomenclature of antimicrobial peptides isolated from frogs of the subfamily Phyllomedusinae.

Doi : https://doi.org/10.1016/j.peptides.2008.06.017

Abstract : A growing number of cationic antimicrobial peptides have been isolated from the skin of hylid frogs belonging to the Phyllomedusinae subfamily. The amino acid sequences of these peptides are currently located in several databases under identifiers with no consistent system of nomenclature to describe them. In order to provide a workable terminology for antimicrobial peptides from Phyllomedusid frogs, we have made a systematic effort to collect, analyze, and classify all the Phyllomedusid peptide sequences available in databases. We propose that frogs belonging to the Phyllomedusinae subfamily should be described by the species names set out in Amphibian Species of the World: http://research.amnh.org/herpetology/amphibia/index.php, American Museum of Natural History, New York, USA. Multiple alignments analysis of at least 80 antimicrobial peptides isolated from 12 Phyllomedusinae species were distributed in seven distinct peptide families including dermaseptin, phylloseptin, plasticin, dermatoxin, phylloxin, hyposin and orphan peptides, and will be considered as the name of the headgroup of each family. The parent peptide's name should be followed by the first upper letter of the species for orthologous peptides and publication date determines priority. For example, the abbreviation B for bicolor and H for hypochondrialis. When two species begin with the same letter, two letters in upper case should be used (the first letter followed by the second or the third letter and so on). For example, the abbreviation DI for distincta, DU for duellmani, VA for vaillanti and VN for vanzolinii. Paralogous peptides should bear letter(s) in upper case followed by numbers.

Paper title : Peptides with differential cytolytic activity from skin secretions of the lemur leaf frog Hylomantis lemur (Hylidae: Phyllomedusinae).

Doi : https://doi.org/10.1016/j.toxicon.2007.04.017

Abstract : Two peptides with differential cytolytic activity against bacteria, a fungus pathogenic to amphibians, and mammalian cells were isolated from norepinephrine-stimulated skin secretions of the Lemur leaf frog Hylomantis lemur Boulenger, 1882. Dermaseptin-L1 (GLWSKIKEAAKAAGKAALNAVTGLVNQGDQPS) was active against the Gram-negative bacterium Escherichia coli (MIC=8 microM) but inactive against the Gram-positive bacterium Staphylococcus aureus. This peptide inhibited growth of zoospores of the chytrid fungus Batrachochytrium dendrobatidis at concentrations above 25 microM but did not completely inhibit growth at 100 microM. Phylloseptin-L1 (LLGMIPLAISAISALSKL.NH2) was active against S. aureus (MIC=8 microM) but was inactive against E. coli. This peptide also inhibited growth of B. dendrobatidis zoospores at concentrations above 25 microM with complete inhibition at 100 microM. Dermaseptin-L1 showed selective cytolytic activity against HepG2 human hepatoma-derived cells (LC50=45 microM) compared with human erythrocytes (LC50=200 microM) whereas phylloseptin-L1 was approximately equipotent against both HepG2 cells (LC50=35 microM) and erythrocytes (LC50=40 microM).