Peptide name : Prepromelittin-related peptide

Source/Organism : Tago frog

Linear/Cyclic : Not found

Chirality : L

Peptide length: 23

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; Hemolytic activity

Amino acid composition bar chart :

Molecular mass : 2392.8802 Dalton

Aliphatic index : 1.487

Instability index : 15.2391

Hydrophobicity (GRAVY) : 0.7304

Isoelectric point : 11.166

Charge (pH 7) : 2.7939

Aromaticity : 0.043

Molar extinction coefficient (cysteine, cystine): (5500, 5500)

Hydrophobic/hydrophilic ratio : 2.28571428

hydrophobic moment : -0.234

Missing amino acid : C,H,Q,M,E,F,D,Y,V

Most occurring amino acid : I

Most occurring amino acid frequency : 4

Least occurring amino acid : P

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.3, 0.4)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](C)N)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)O)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)[C@@H](C)CC

1 : Thomas S, et al. CAMP: a useful resource for research on antimicrobial peptides. Nucleic Acids Res. 2010; 38:D774-80. doi: 10.1093/nar/gkp1021

2 : Conlon JM, et al. A melittin-related peptide from the skin of the Japanese frog, Rana tagoi, with antimicrobial and cytolytic properties. Biochem Biophys Res Commun. 2003; 306:496-500. doi: 10.1016/s0006-291x(03)00999-9

Paper title : CAMP: a useful resource for research on antimicrobial peptides.

Doi : https://doi.org/10.1093/nar/gkp1021

Abstract : Antimicrobial peptides (AMPs) are gaining popularity as better substitute to antibiotics. These peptides are shown to be active against several bacteria, fungi, viruses, protozoa and cancerous cells. Understanding the role of primary structure of AMPs in their specificity and activity is essential for their rational design as drugs. Collection of Anti-Microbial Peptides (CAMP) is a free online database that has been developed for advancement of the present understanding on antimicrobial peptides. It is manually curated and currently holds 3782 antimicrobial sequences. These sequences are divided into experimentally validated (patents and non-patents: 2766) and predicted (1016) datasets based on their reference literature. Information like source organism, activity (MIC values), reference literature, target and non-target organisms of AMPs are captured in the database. The experimentally validated dataset has been further used to develop prediction tools for AMPs based on the machine learning algorithms like Random Forests (RF), Support Vector Machines (SVM) and Discriminant Analysis (DA). The prediction models gave accuracies of 93.2% (RF), 91.5% (SVM) and 87.5% (DA) on the test datasets. The prediction and sequence analysis tools, including BLAST, are integrated in the database. CAMP will be a useful database for study of sequence-activity and -specificity relationships in AMPs. CAMP is freely available at http://www.bicnirrh.res.in/antimicrobial.

Paper title : A melittin-related peptide from the skin of the Japanese frog, Rana tagoi, with antimicrobial and cytolytic properties.

Doi : https://doi.org/10.1016/s0006-291x(03)00999-9

Abstract : Two peptides with antimicrobial and cytolytic properties were purified from an extract of the skin of Tago's brown frog Rana tagoi. The primary structure of one peptide (FLPILGKLLS(10)GIL.NH(2)) identifies it as a member of the temporin family, whereas the second peptide (AIGSILGALA(10)KGLPTLISWI(20)KNR.NH(2)) displays 78% sequence identity to melittin from the venom of the honeybee Apis florea. Compared with melittin, the melittin-related peptide (MRP) was equipotent in inhibiting the growth of the Gram-positive bacterium Staphylococcus aureus, 5-fold less potent against the Gram-negative bacterium Escherichia coli and against the fungal pathogen, Candida albicans. MRP was 13-fold less hemolytic than melittin against human erythrocytes and 4- and 5-fold less cytolytic against mouse EL4 T-lymphoma-derived cells and L929 fibroblasts, respectively. However, at non-cytotoxic concentrations (<or=8 microM), MRP did not protect HeLa cells from cell death produced by human rhinovirus type 2 infection.