dbACP: A Comprehensive Database of Anti-Cancer Peptides

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

Pubmed Id : 17194500

Uniprot : Not available

PDB : Not available

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.