DFBP ID - DFBPAMIC0019(Antimicrobial peptide)

DFBP ID DFBPAMIC0019 Peptide sequence GLFLDTLKGAAKDVAGKLEGLKCKITGCKLP Type Native peptide Peptide/Function name Antimicrobial peptide, RANATUERIN 2

Function-activity relationship

Main bioactivity Antimicrobial activity Otheir bioactivity Anticancer activity [D1]

Calculated physicochemical properties

Three-letter amino acid Gly-Leu-Phe-Leu-Asp-Thr-Leu-Lys-Gly-Ala-Ala-Lys-Asp-Val-Ala-Gly-Lys-Leu-Glu-Gly-Leu-Lys-Cys-Lys-Ile-Thr-Gly-Cys-Lys-Leu-Pro Single-letter amino acid GLFLDTLKGAAKDVAGKLEGLKCKITGCKLP Peptide length 31 Peptide mass Experimental mass Theoretical mass N.D 3188.85 Da c Net charge +3 Isoelectric point (pI) 9.57 c IC50 N.D pIC50 N.D GRAVY 0.1871 c Hydrophilic residue ratio 58.06% c Peptide calculator To calculate the physicochemical properties of bioactive peptide.

Peptide source & Food-borne protein(s) search

Classification Animal Organism/Source American bull frog, Rana catesbeiana Precursor protein The extract of the skin of the adult american bullfrog Residue position N.D Precursor protein(s) search No matching precursor protein found Link-research Inductive analysis There are no literature reports on the discovery of this sequence in other food-source proteins.

Biological/Functional activity & target protein

Antimicrobial activity Minimal inhibitory concentrations (MIC) of RANATUERIN 2 for three bacterial strains:      S. aureus ---------> 60 uM. Specific target protein(s) N.D

Taste properties & Structure

Bitterness Literature report N.D Bitter prediction tools No prediction can be made about the peptide bitterness. prediction SMILES NCC(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCCCN)C(=O)NCC(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(C)C(=O)NCC(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)NCC(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)NCC(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)O

Preparation method

Mode of preparation Extract of the skin tissue without enzyme Enzyme(s)/starter culture Skin (176 g) was removed from pithed adult specimens of R. catesbeiana of both sexes (n=6) and immediately frozen on dry-ice. The tissue was stored at 55°C until time of extraction. The tissue was extracted by homogenization in ethanol/0.7 M HCl (3:1 v/v; 1800 ml) at 0 °C using a Waring blender.

Stability & Cytotoxicity

Peptide stability Literature report: Not measured EHP-Tool: Enzymatic Hydrolysis Prediction Tool (EHP-Tool) Peptide cytotoxicity Literature report: The hemolytic activity towards human erythrocytes. Prediction: ToxinPred

Additional information

Additional information N.D

Database cross-references

DFBP [D1] DFBPANCA0602

BIOPEP-UWM [D2] -

APD [D3] -

BioPepDB [D4] -

MBPDB [D5] -

Reference(s)

Primary literature Goraya J, Knoop FC, Conlon JM. Ranatuerins: antimicrobial peptides isolated from the skin of the American bullfrog, Rana catesbeiana. Biochem Biophys Res Commun. 1998 Sep 29;250(3):589-92. PMID: 9784389 DOI: 10.1006/bbrc.1998.9362 Other literature(s) [1] Clark D P, Durell S, Maloy W L, et al. Ranalexin. A novel antimicrobial peptide from bullfrog (Rana catesbeiana) skin, structurally related to the bacterial antibiotic, polymyxin[J]. Journal of Biological Chemistry, 1994, 269(14):10849. PubDate 1998