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 - DFBPAMIC0003(Antimicrobial peptide)

DFBP ID	DFBPAMIC0003
Peptide sequence	RFRPPIRRPPIRPPFYPPFRPPIRPPIFPPIRPPFRPPLGPFP
Type	Native peptide
Peptide/Function name	Antimicrobial peptide, Bactenecin 5

Function-activity relationship

Main bioactivity	Antimicrobial activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Arg-Phe-Arg-Pro-Pro-Ile-Arg-Arg-Pro-Pro-Ile-Arg-Pro-Pro-Phe-Tyr-Pro-Pro-Phe-Arg-Pro-Pro-Ile-Arg-Pro-Pro-Ile-Phe-Pro-Pro-Ile-Arg-Pro-Pro-Phe-Arg-Pro-Pro-Leu-Gly-Pro-Phe-Pro

Single-letter amino acid

RFRPPIRRPPIRPPFYPPFRPPIRPPIFPPIRPPFRPPLGPFP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	5148.18 Da ^c

Net charge

Isoelectric point (pI)

13.04 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.7233^c

Hydrophilic residue ratio

76.74%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bos taurus (Bovine)
Precursor protein	Extracts of granules of bovine neutrophils
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR17968 ---- Animal proteins ---- Cathelicidin-2
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

(1) Exerts, in vitro, a potent antimicrobial activity. probably due to an impairment of the function of the respiratory chain and of energy-dependent activities in the inner membrane of susceptible microorganisms.
(2) Bactenecin 5 efficiently kill Escherichia coli, Salmonella typhimurium, and Klebsiella
pneumoniae. It also arrest the growth of Enterobacter cloacae (MICs, 25 to 200 ug/ml) but not of Proteus vulgaris, Staphylococcus aureus, and Streptococcus agalactiae (MIC, >200 ug/ml). The datas as follows:
      Organism and strain                          Mueller-Hinton(ug/ml)        Iso-Sensitest(ug/ml)
         (1) Escherichia coli ATCC 25922                     12                            12
         (2) Salmonella typhimurium LT2                      12                            12
         (3) Salmonella typhimurium ATCC 14028               25                            25
         (4) Klebsiella pneumoniae ATCC 13883                25                            12
         (5) Enterobacter cloacae ATCC 13047              25                            25
         (6) Proteus vulgaris ATCC 13315                     >200                          >200
         (7) Pseudomonas aeruginosa ATCC 7700              >200                          >200
         (8) Staphylococcus epidermidis ATCC 12228         >200                          >200
         (9) Staphylococcus aureus ATCC 25923              >200                          >200
         (10) Streptococcus agalactiae ATCC 13813          >200                          >200

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])(Cc1ccccc1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(C)C)C(=O)NCC(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N1[C@@]([H])(CCC1)C(=O)O

Preparation method

Mode of preparation	Preparation of the granular extract
Enzyme(s)/starter culture	No enzyme (Bovine neutrophils (about 1.5 x 1010 per batch) were isolated from freshly collected blood, and the total granular population was separated from postnuclear supernatants as previously described ^[1]).

Stability & Cytotoxicity

Peptide stability

Literature report:	N.D
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	Gennaro R, Skerlavaj B, Romeo D. Purification, composition, and activity of two bactenecins, antibacterial peptides of bovine neutrophils. Infect Immun. 1989 Oct;57(10):3142-6. PMID: 2777377 DOI: 10.1128/IAI.57.10.3142-3146.1989
Other literature(s)	[1] 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. [2] Storici P, Tossi A, Lenarcic B, et al. Purification and structural characterization of bovine cathelicidins, precursors of antimicrobial peptides[J]. Febs Journal, 1996, 238(3):769-776.
PubDate	1989