dbacp05916
General Description
Peptide name : Raniseptin PL
Source/Organism : Skin secretions, the banana tree dwelling frog, Trinidad, South America
Linear/Cyclic : Not found
Chirality : Not found
Sequence Information
Sequence : GVFDTVKKIGKAVGKFALGVAKNYLNS
Peptide length: 27
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 : LC50 : < 30 μM
Cell line : HT29
Cancer type : Not found
Other activity : Anti-bacterial activity
Physicochemical Properties
Amino acid composition bar chart :
Molecular mass : 2825.3071 Dalton
Aliphatic index : 0.974
Instability index : -5.0111
Hydrophobicity (GRAVY) : 0.2037
Isoelectric point : 10.000
Charge (pH 7) : 3.7552
Aromaticity : 0.111
Molar extinction coefficient (cysteine, cystine): (1490, 1490)
Hydrophobic/hydrophilic ratio : 1.45454545
hydrophobic moment : -0.974
Missing amino acid : C,R,W,H,Q,P,M,E
Most occurring amino acid : K
Most occurring amino acid frequency : 5
Least occurring amino acid : D
Least occurring amino acid frequency : 1
Structural Information
3D structure :
Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.3, 0.4)
SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](NC(=O)CN)C(C)C)[C@@H](C)O)C(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)O)C(C)C)C(C)C
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | CEHHHHHHHHHHHHHHHHHHHTTCTTT |
| Chou-Fasman (CF) | EEEEEEHHHHHHCCCCEEHHHHCCCCC |
| Neural Network (NN) | CCCCHHHCCCCHHHHHHHHHHHHCCCC |
| Joint/Consensus | CCCCHHHHHHHHHHHHHHHHHHCCCCC |
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 : Conlon JM, et al. Multifunctional host-defense peptides isolated from skin secretions of the banana tree dwelling frog Boana platanera (Hylidae; Hylinae). Biochimie. 2024; 223:23-30. doi: 10.1016/j.biochi.2024.03.012
Literature
Paper title : Multifunctional host-defense peptides isolated from skin secretions of the banana tree dwelling frog Boana platanera (Hylidae; Hylinae).
Doi : https://doi.org/10.1016/j.biochi.2024.03.012
Abstract : Five host-defense peptides (figainin 2PL, hylin PL, raniseptin PL, plasticin PL, and peptide YL) were isolated from norepinephrine-stimulated skin secretions of the banana tree dwelling frog Boana platanera (Hylidae; Hylinae) collected in Trinidad. Raniseptin PL (GVFDTVKKIGKAVGKFALGVAKNYLNS.NH<sub>2</sub>) and figainin 2PL (FLGTVLKLGKAIAKTVVPMLTNAMQPKQ. NH<sub>2</sub>) showed potent and rapid bactericidal activity against a range of clinically relevant Gram-positive and Gram-negative ESKAPE + pathogens and Clostridioides difficile. The peptides also showed potent cytotoxic activity (LC<sub>50</sub> values < 30 μM) against A549, MDA-MB-231 and HT29 human tumor-derived cell lines but appreciably lower hemolytic activity against mouse erythrocytes (LC<sub>50</sub> = 262 ± 14 μM for raniseptin PL and 157 ± 16 μM for figainin 2PL). Hylin PL (FLGLIPALAGAIGNLIK.NH<sub>2</sub>) showed relatively weak activity against microorganisms but was more hemolytic. The glycine-leucine-rich peptide with structural similarity to the plasticins (GLLSTVGGLVGGLLNNLGL.NH<sub>2</sub>) and the non-cytotoxic peptide YL (YVPGVIESLL.NH<sub>2</sub>) lacked antimicrobial and cytotoxic activities. Hylin PL, raniseptinPL and peptide YL stimulated the rate of release of insulin from BRIN-BD11 clonal β-cells at concentrations ≥100 nM. Peptide YL was the most effective (2.3-fold increase compared with basal rate at 1 μM concentration) and may represent a template for the design of a new class of incretin-based anti-diabetic drugs.