dbACP: A Comprehensive Database of Anti-Cancer Peptides

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

Pubmed Id : 38561076

Uniprot : Not available

PDB : Not available

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 &lt; 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.