dbacp02639
General Description
Peptide name : Defensin (Galiomicin)
Source/Organism : Greater wax moth
Linear/Cyclic : Not specified
Chirality : Not found
Sequence Information
Sequence : MAKNFQSVLLLVCLSFLVIVSSPQNAVQADTLIGSCVWGATNYTSDCNAECKRRGYKGGHCGSFLNVNCWCE
Peptide length: 72
C-terminal modification: Not specified
N-terminal modification : Not found
Non-natural peptide information: None
Activity Information
Assay type : Radial diffusion assay
Assay time : 48h
Activity : Not found
Cell line : Not found
Cancer type : Not specified
Other activity : Anti-microbial activity
Physicochemical Properties
Amino acid composition bar chart :
Molecular mass : 7822.9335 Dalton
Aliphatic index : 0.838
Instability index : 42.5181
Hydrophobicity (GRAVY) : 0.2264
Isoelectric point : 7.5426
Charge (pH 7) : 0.5263
Aromaticity : 0.097
Molar extinction coefficient (cysteine, cystine): (13980, 14355)
Hydrophobic/hydrophilic ratio : 1.32258064
hydrophobic moment : 0.435
Missing amino acid : None
Most occurring amino acid : S
Most occurring amino acid frequency : 7
Least occurring amino acid : M
Least occurring amino acid frequency : 1
Structural Information
3D structure :
Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.3, 0.3)
SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@@H](N)CCSC)C(C)C)C(C)C)C(C)C)[C@@H](C)CC)C(C)C)C(C)C)[C@@H](C)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)NCC(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)NCC(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](CS)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(=O)O)C(=O)O)C(C)C)[C@@H](C)O)[C@@H](C)O)C(C)C
Secondary Structure :
| Method | Prediction |
|---|---|
| GOR | HHHHHCHEEEEEEEEEEEEEECCCCCHEEEEEEEEEEETCCCCCCTTTHHHHHTTTTTCCEEEEETTTTHHH |
| Chou-Fasman (CF) | CCCCEEEEEEEEEEEEEEEECCCHHHHHHEEEEEEEEECEEEEECHHHHHHCCCCCCCCCEEEEEEEECCCC |
| Neural Network (NN) | HHHHHHHHHHHHHHHHEEECCCCCCCCCCCCCEEEEEECCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC |
| Joint/Consensus | HHHHHCCEEEEEEEEEEEEECCCCCCCCCEEEEEEEEECCCCCCCCCCCCCCCCCCCCCCEEEEECCCCCCC |
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 : Cytryńska M, et al. Purification and characterization of eight peptides from Galleria mellonella immune hemolymph. Peptides. 2007; 28:533-46. doi: 10.1016/j.peptides.2006.11.010
Literature
Paper title : Purification and characterization of eight peptides from Galleria mellonella immune hemolymph.
Doi : https://doi.org/10.1016/j.peptides.2006.11.010
Abstract : Defense peptides play a crucial role in insect innate immunity against invading pathogens. From the hemolymph of immune-challenged greater wax moth, Galleria mellonella (Gm) larvae, eight peptides were isolated and characterized. Purified Gm peptides differ considerably in amino acid sequences, isoelectric point values and antimicrobial activity spectrum. Five of them, Gm proline-rich peptide 2, Gm defensin-like peptide, Gm anionic peptides 1 and 2 and Gm apolipophoricin, were not described earlier in G. mellonella. Three others, Gm proline-rich peptide 1, Gm cecropin D-like peptide and Galleria defensin, were identical with known G. mellonella peptides. Gm proline-rich peptides 1 and 2 and Gm anionic peptide 2, had unique amino acid sequences and no homologs have been found for these peptides. Antimicrobial activity of purified peptides was tested against gram-negative and gram-positive bacteria, yeast and filamentous fungi. The most effective was Gm defensin-like peptide which inhibited fungal and sensitive bacteria growth in a concentration of 2.9 and 1.9 microM, respectively. This is the first report describing at least a part of defense peptide repertoire of G. mellonella immune hemolymph.