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
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).