Peptide name : EP5-1

Source/Organism : Redworms, brandling worms, "tiger worms" and red wiggler worms

Linear/Cyclic : Not found

Chirality : L

Peptide length: 5

C-terminal modification: Not found

N-terminal modification : Free

Non-natural peptide information: None

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Not found

Cancer type : Fibrosarcoma

Other activity : Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 407.4426 Dalton

Aliphatic index : 0.4

Instability index : 95.88

Hydrophobicity (GRAVY) : 0.98

Isoelectric point : 5.5615

Charge (pH 7) : -0.214

Aromaticity : 0

Molar extinction coefficient (cysteine, cystine): (0, 0)

Hydrophobic/hydrophilic ratio : 4

hydrophobic moment : 0.5422

Missing amino acid : W,T,P,I,M,E,K,F,D,N,R,H,Q,Y,L,V

Most occurring amino acid : A

Most occurring amino acid frequency : 2

Least occurring amino acid : C

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.4, 0.4, 0)

SMILES Notation: C[C@H](N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)NCC(=O)O

1 : Liu YQ, et al. Purification of a novel antibacterial short peptide in earthworm Eisenia foetida. Acta Biochim Biophys Sin (Shanghai). 2004; 36:297-302. doi: 10.1093/abbs/36.4.297

2 : Wang G, et al. APD2: the updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res. 2009; 37:D933-7. doi: 10.1093/nar/gkn823

Paper title : Purification of a novel antibacterial short peptide in earthworm Eisenia foetida.

Doi : https://doi.org/10.1093/abbs/36.4.297

Abstract : A novel antimicrobial short peptide was purified from earthworm (Eisenia foetida) by a five-step protocol including ammonium sulfate precipitation, ultrafiltration, DE-52 ion exchange chromatography, Sephadex G-10 column chromatography, and C-18 reversed-phase HPLC techniques. The purified peptide was applied to the MALDI-TOP MS to determine the molecular mass and was also subjected to TOF MS-MS analysis to determine the amino acid sequence. As a result, a novel antibacterial peptide, named OEP3121, was obtained, with the molecular mass of 510.8 Da and the sequence being "ACSAG".

Paper title : APD2: the updated antimicrobial peptide database and its application in peptide design.

Doi : https://doi.org/10.1093/nar/gkn823

Abstract : The antimicrobial peptide database (APD, http://aps.unmc.edu/AP/main.php) has been updated and expanded. It now hosts 1228 entries with 65 anticancer, 76 antiviral (53 anti-HIV), 327 antifungal and 944 antibacterial peptides. The second version of our database (APD2) allows users to search peptide families (e.g. bacteriocins, cyclotides, or defensins), peptide sources (e.g. fish, frogs or chicken), post-translationally modified peptides (e.g. amidation, oxidation, lipidation, glycosylation or d-amino acids), and peptide binding targets (e.g. membranes, proteins, DNA/RNA, LPS or sugars). Statistical analyses reveal that the frequently used amino acid residues (>10%) are Ala and Gly in bacterial peptides, Cys and Gly in plant peptides, Ala, Gly and Lys in insect peptides, and Leu, Ala, Gly and Lys in amphibian peptides. Using frequently occurring residues, we demonstrate database-aided peptide design in different ways. Among the three peptides designed, GLK-19 showed a higher activity against Escherichia coli than human LL-37.