Peptide name : Alloferon 1

Source/Organism : Blow fly

Linear/Cyclic : Not found

Chirality : L

Peptide length: 13

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 : Skin cancer

Other activity : Anti-microbial activity; Spermicidal action; Anti-HIV activity

Amino acid composition bar chart :

Molecular mass : 1265.2975 Dalton

Aliphatic index : 0.446

Instability index : -22.676

Hydrophobicity (GRAVY) : -0.823

Isoelectric point : 7.0977

Charge (pH 7) : 0.1088

Aromaticity : 0

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

Hydrophobic/hydrophilic ratio : 1.16666666

hydrophobic moment : -0.819

Missing amino acid : C,R,W,T,P,M,I,E,K,F,D,Y,L,N,A

Most occurring amino acid : G

Most occurring amino acid frequency : 5

Least occurring amino acid : S

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0, 0.4, 0.1)

SMILES Notation: CC(C)[C@H](NC(=O)CNC(=O)[C@@H](N)Cc1c[nH]cn1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](Cc1c[nH]cn1)C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)NCC(=O)N[C@H](C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)NCC(=O)O)C(C)C

1 : 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

2 : Chernysh S, et al. Antiviral and antitumor peptides from insects. Proc Natl Acad Sci U S A. 2002; 99:12628-32. doi: 10.1073/pnas.192301899

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.

Paper title : Antiviral and antitumor peptides from insects.

Doi : https://doi.org/10.1073/pnas.192301899

Abstract : Insects can rapidly clear microbial infections by producing a variety of immune-induced molecules including antibacterial and/or antifungal peptides/polypeptides. In this report, we present the isolation, structural characterization, and biological properties of two variants of a group of bioactive, slightly cationic peptides, referred to as alloferons. Two peptides were isolated from the blood of an experimentally infected insect, the blow fly Calliphora vicina (Diptera), with the following amino acid sequences: HGVSGHGQHGVHG (alloferon 1) and GVSGHGQHGVHG (alloferon 2). Although these peptides have no clear homologies with known immune response modifiers, protein database searches established some structural similarities with proteins containing amino acid stretches similar to alloferon. In vitro experiments reveal that the synthetic version of alloferon has stimulatory activities on natural killer lymphocytes, whereas in vivo trials indicate induction of IFN production in mice after treatments with synthetic alloferon. Additional in vivo experiments in mice indicate that alloferon has antiviral and antitumoral capabilities. Taken together, these results suggest that this peptide, which has immunomodulatory properties, may have therapeutic capacities. The fact that insects may produce cytokine-like materials modulating basic mechanisms for human immunity suggests a source of anti-infection and antitumoral biopharmaceuticals.