dbacp04476
General Description
Peptide name : Magainin 2
Source/Organism : African clawed frog
Linear/Cyclic : Linear
Chirality : L
Sequence Information
Sequence : GIGKFLHSAKKFGKAFVGEIMNS
Peptide length: 23
C-terminal modification: Linear
N-terminal modification : Free
Non-natural peptide information: None
Activity Information
Assay type : WST-1 assay
Assay time : Not found
Activity : IC50 : > 60 µM
Cell line : HeLa
Cancer type : Pancreatic cancer
Other activity : Anti-microbial activity
Physicochemical Properties
Amino acid composition bar chart :
Molecular mass : 2466.8972 Dalton
Aliphatic index : 0.721
Instability index : -0.1043
Hydrophobicity (GRAVY) : 0.0826
Isoelectric point : 10.001
Charge (pH 7) : 2.8461
Aromaticity : 0.130
Molar extinction coefficient (cysteine, cystine): (0, 0)
Hydrophobic/hydrophilic ratio : 1.55555555
hydrophobic moment : -0.123
Missing amino acid : C,R,W,Q,T,P,D,Y
Most occurring amino acid : G
Most occurring amino acid frequency : 4
Least occurring amino acid : L
Least occurring amino acid frequency : 1
Structural Information
3D structure :
Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.3, 0.3)
SMILES Notation: CC[C@H](C)[C@H](NC(=O)CN)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](Cc1ccccc1)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)O)[C@@H](C)CC)C(C)C
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | THHHHHHHHHHHHHHHHHHHHHT |
| Chou-Fasman (CF) | EEHHHHHHHHHHHHEEECCCCCC |
| Neural Network (NN) | CCCHHHHHHCCCCCCHHHHHCCC |
| Joint/Consensus | CCHHHHHHHHHHHHCHHHHHCCC |
Molecular Descriptors and ADMET Properties
Molecular Descriptors: Click here to download
ADMET Properties: Click here to download
Cross Referencing databases
Reference
1 : Hu J, et al. Designed antimicrobial and antitumor peptides with high selectivity. Biomacromolecules. 2011; 12:3839-43. doi: 10.1021/bm201098j
Literature
Paper title : Designed antimicrobial and antitumor peptides with high selectivity.
Doi : https://doi.org/10.1021/bm201098j
Abstract : We report a new class of cationic amphiphilic peptides with short sequences, G(IIKK)(n)I-NH(2) (n = 1-4), that can kill Gram-positive and Gram-negative bacteria as effectively as several well-known antimicrobial peptides and antibiotics. In addition, some of these peptides possess potent antitumor activities against cancer cell lines. Moreover, their hemolytic activities against human red blood cells (hRBCs) remain remarkably low even at some 10-fold bactericidal minimum inhibitory concentrations (MICs). When bacteria or tumor cells are cocultured with NIH 3T3 fibroblast cells, G(IIKK)(3)I-NH(2) showed fast and strong selectivity against microbial or tumor cells, without any adverse effect on NIH 3T3 cells. The high selectivity and associated features are attributed to two design tactics: the use of Ile residues rather than Leu and the perturbation of the hydrophobic face of the helical structure with the insertion of a positively charged Lys residue. This class of simple peptides hence offers new opportunities in the development of cost-effective and highly selective antimicrobial and antitumor peptide-based treatments.