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 - DFBPAMIC0030(Antimicrobial peptide)

DFBP ID	DFBPAMIC0030
Peptide sequence	VRRFPWWWPFLRR
Type	Native peptide
Peptide/Function name	Antimicrobial peptide, Tritrpticin

Function-activity relationship

Main bioactivity	Antimicrobial activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Val-Arg-Arg-Phe-Pro-Trp-Trp-Trp-Pro-Phe-Leu-Arg-Arg

Single-letter amino acid

VRRFPWWWPFLRR

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1902.27 Da ^c

Net charge

Isoelectric point (pI)

12.98 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.7923^c

Hydrophilic residue ratio

69.23%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Synthetic fragment of porcine cathelicidin
Precursor protein	A cDNA library form the porcine bone marrow
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR9113 ---- Animal proteins ---- Prophenin and tritrpticin precursor Source.2: DFBPPR9239 ---- Animal proteins ---- Prophenin-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) It showed potency against Escherichia coli, Pseudomonas aeruginosa, Kiebsiella pneumonia, Staphylococcus epidermidis, Proteus mirabilis, and Streptococcus group D as well as Aspergillus fumigatus.

Bacterias	Inhibitory activity	Method
E.coli	50ug/well--->10 mm, 5ug/well--->6 mm	Zone inhibition assay
E.coli	5 mm
P. aeruginosa	3 mm
K. pneumoniae	7 mm
S. epidermidis	5 mm
P. mirabilis	1 mm
Streptococcus (Group D)	4 mm
Aspergillus fumigatus	250 ug/ml	MIC assay
Candida albicans	1000 ug/ml	MIC assay

(2) The peptide remained active against bacteria after deleting the N-terminal 6 residues^[1].

Specific target protein(s)

N.D

Taste properties & Structure

Bitterness

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

SMILES

N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(=CN2)C1=C2C=CC=C1)C(=O)N[C@@]([H])(CC(=CN2)C1=C2C=CC=C1)C(=O)N[C@@]([H])(CC(=CN2)C1=C2C=CC=C1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)O

Preparation method

Mode of preparation	Synthesis
Enzyme(s)/starter culture	Peptide synthesis: The peptides were synthesized by Fmoc solid-phase synthesis using Opfp or Odhbt active esters on a Milligen 9050 peptide synthesizer (Perseptive Biosystems, Framingham, MA).

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	Lawyer C, Pai S, Watabe M, Borgia P, Mashimo T, Eagleton L, Watabe K. Antimicrobial activity of a 13 amino acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides. FEBS Lett. 1996 Jul 15;390(1):95-8. PMID: 8706838 DOI: 10.1016/0014-5793(96)00637-0
Other literature(s)	[1] Nagpal S, Gupta V, Kaur K J, et al. Structure-function analysis of tritrypticin, an antibacterial peptide of innate immune origin[J]. Journal of Biological Chemistry, 1999, 274(33):23296. [2] Borgia P T, Dodge C L. Characterization of Aspergillus nidulans mutants deficient in cell wall chitin or glucan[J]. Journal of Bacteriology, 1992, 174(2):377-83.
PubDate	1996