Peptide properties

1Top 2Function-activity relationship 3Calculated physicochemical properties 4Peptide source & Food-borne protein(s) search 5Biological/Functional activity & target protein 6Taste properties & Structure 7Preparation method 8Stability & Cytotoxicity 9Additional information 10Database cross-references 11Reference(s)

List of peptide properties

DFBP ID - DFBPAMIC0002(Antimicrobial peptide)

DFBP ID	DFBPAMIC0002
Peptide sequence	RLCRIVVIRVCR
Type	Native peptide
Peptide/Function name	Antimicrobial peptide, Bactenecin

Function-activity relationship

Main bioactivity	Antimicrobial activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Arg-Leu-Cys-Arg-Ile-Val-Val-Ile-Arg-Val-Cys-Arg

Single-letter amino acid

RLCRIVVIRVCR

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1485.91 Da ^c

Net charge

Isoelectric point (pI)

12.02 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

1.0333^c

Hydrophilic residue ratio

50%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bos taurus (Bovine)
Precursor protein	The acid extract of bovine neutrophil granules
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR17583 ---- Animal proteins ---- Cathelicidin-1
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

Staphylococcus aureus ATCC 25923 and Escherichia coli ATCC 25922 were grown in Iso-Sensitest Staphylococcus aureus ATCC 25923 and Escherichia coli ATCC 25922 were grown in Iso-Sensites broth(Oxoid, UK), and the minimal inhibitory concentration of the bactenecin was assayed by a microdilutionsusceptibility test ^[1].The bactericidal activity was evaluated by counting on plates the colony forming units (CFU)of bacteria treatedat 37 ℃ for 0.5 or 2 h with various concentrationsof bactenecin in a medium preventing bacterial growth (PBS: 10 mM sodium phosphate, pH 7.2, 127 mM NaC1, 3.8 mM KCl, 0.5 mM Mg₂S0₄, 0.9mM CaCl₂). From an acid extract of bovine neutrophil granuleswe have purified over 2000-fold a dodecapeptide (Bactenecin) exhibiting bactericidal activity against both Escherichia coli and Staphylococcus aureus at 10-⁷-10^-5 M concentration.

Specific target protein(s)

N.D

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Bitter taste ^prediction

SMILES

N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)O

Preparation method

Mode of preparation	The acid extract of bovine neutrophil granules
Enzyme(s)/starter culture	No enzyme (Granules of peripheral bovine neutrophils were extracted in 0.2 M sodium acetate, 5 mM EDTA, pH 4, as previously reported^[2], and the extracted proteins were fractionated to yield an over 2000-fold purified antibacterial dodecapeptide.)

Stability & Cytotoxicity

Peptide stability

Literature report:	Not&nbspmeasure
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	N.D
Prediction:	ToxinPred

Additional information

N.D

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Romeo D, Skerlavaj B, Bolognesi M, Gennaro R. Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils. J Biol Chem. 1988 Jul 15;263(20):9573-5. PMID: 3290210
Other literature(s)	[1] Savoini A, Marzari R, Dolzani L, et al. Wide-spectrum antibiotic activity of bovine granulocyte polypeptides[J]. Antimicrob Agents Chemother, 1984, 26(3):405-7. [2] Gennaro R, Dolzani L, Romeo D. Potency of bactericidal proteins purified from the large granules of bovine neutrophils[J]. Infection & Immunity, 1983, 40(2):684-90.
PubDate	1988