dbacp05548
General Description
Peptide name : Phylloseptin-PHa
Source/Organism : Northern orange-legged leaf frog
Linear/Cyclic : Not found
Chirality : Not found
Sequence Information
Sequence : FLSLIPAAISAVSALANHF
Peptide length: 19
C-terminal modification: Not found
N-terminal modification : Amidation
Non-natural peptide information: None
Activity Information
Assay type : MTT assay, Lactate dehydrogenase (LDH) assay
Assay time : Not found
Activity : LD50 : < 5 µM
Cell line : MDA-MB-435
Cancer type : Melanocyte
Other activity : Anti-microbial activity
Physicochemical Properties
Amino acid composition bar chart :
Molecular mass : 1942.2604 Dalton
Aliphatic index : 1.442
Instability index : 12.6368
Hydrophobicity (GRAVY) : 1.5
Isoelectric point : 6.7411
Charge (pH 7) : -0.1527
Aromaticity : 0.105
Molar extinction coefficient (cysteine, cystine): (0, 0)
Hydrophobic/hydrophilic ratio : 2.8
hydrophobic moment : 1.346
Missing amino acid : C,R,W,Q,T,M,E,K,D,Y,G
Most occurring amino acid : A
Most occurring amino acid frequency : 5
Least occurring amino acid : P
Least occurring amino acid frequency : 1
Structural Information
3D structure :
Secondary structure fraction (Helix, Turn, Sheet): (0.4, 0.2, 0.4)
SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)Cc1ccccc1)[C@@H](C)CC)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](Cc1ccccc1)C(=O)O)C(C)C
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | EEEECHHHHHHHHHHHHHH |
| Chou-Fasman (CF) | EEEHHHHHEECCHHHHCCC |
| Neural Network (NN) | CCCCCCCHHHHHHHHHHHH |
| Joint/Consensus | EEECCHHHHHHHHHHHHHH |
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 : Liu Y, et al. Structure-activity relationship of an antimicrobial peptide, Phylloseptin-PHa: balance of hydrophobicity and charge determines the selectivity of bioactivities. Drug Des Devel Ther. 2019; 13:447-458. doi: 10.2147/DDDT.S191072
Literature
Paper title : Structure-activity relationship of an antimicrobial peptide, Phylloseptin-PHa: balance of hydrophobicity and charge determines the selectivity of bioactivities.
Doi : https://doi.org/10.2147/DDDT.S191072
Abstract : BACKGROUND: Antimicrobial peptides (AMPs) from the skin secretions of amphibians are now considered as a potential alternative to conventional antibiotics. Phylloseptins are a family of AMPs identified in the skin secretions of Phyllomedusinae tree frogs which exhibit highly conserved structural characteristics. This study examines the structure-activity relationship of the newly discovered phylloseptin, Phylloseptin-PHa (PSPHa) from Pithecopus hypochondrialis. MATERIALS AND METHODS: PSPHa and modified analogs were produced by solid phase synthesis and purified by reverse-phase HPLC. Rationally designed modified analogs incorporating changes in significant physicochemical parameters such as hydrophobicity, hydrophobic moment and net charge were investigated to determine their influence on secondary structure, antimicrobial activity, membrane permeabilization and cytotoxicity. RESULTS: Overall, we found that when rationally designing AMPs by altering their primary structure it is important to keep a balance between hydrophobicity and charge. CONCLUSION: This study provides new insights which will help in the future development of AMPs as alternatives to conventional antibiotics for the treatment of Staphylococcus aureus and methicillin-resistant S. aureus infections.