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 - DFBPAMIC0517(Antimicrobial peptide)

DFBP ID	DFBPAMIC0517
Peptide sequence	DFHINQ
Type	Native peptide
Peptide/Function name	Antimicrobial peptide

Function-activity relationship

Main bioactivity	Antimicrobial activity
Otheir bioactivity	ACE-inhibitory activity ^[D1], Anticancer activity ^[D2], Multifunctional activity ^[D3]

Calculated physicochemical properties

Three-letter amino acid

Asp-Phe-His-Ile-Asn-Gln

Single-letter amino acid

DFHINQ

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	772.81 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

4.96 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-1.0667^c

Hydrophilic residue ratio

33.33%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Beef sarcoplasmic
Precursor protein	Beef sarcoplasmic protein hydrolysates
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

Table 1 show the effects of ACE inhibitory peptide DFHINQ on three Gram-positive (B. cereus, L. monocytogens, and S. aureus) and three Gram-negative (S. Typhimurium, E. Coli, and P. aeruginosa) pathogens. Only E. coli was sensitive against peptide DFHINQ at all treated concentrations.

Table 1. Antimicrobial activity of the synthetic peptide DFHINQ on six pathogens
Concentration (μg)	Microorganisms
Concentration (μg)	*S. Typhimurium*	*B. cereus*	*E. coli*	*L. monoytogenes*	*S. aureus*	*P. aeruginosa*
100	—	—	+	—	—	—
200	—	—	+	—	—	—
400	—	+	+	—	—	+
+, Sensitive (9–12 mm inhibition); –, not detected.

Specific target protein(s)

N.D

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Non-bitter taste ^prediction

SMILES

N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CC(=O)N)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Hydrolysis with commercial enzymes (proteinase alcalase).

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

The ACE inhibitory peptides identified from beef sarcoplasmic protein hydrolysates have both antimicrobial and cancer cell cytotoxic effects. The ACE inhibitory peptides can be expected to possess other biological functions and used as functional materials for food industry.

Database cross-references

DFBP

[D1]	DFBPACEI0113
[D2]	DFBPANCA0331
[D3]	DFBPMUFU0047

[D4]

[D5]

[D6]

[D7]

Reference(s)

Primary literature	Jang, A., Jo, C., Kang, K.-S., Lee, M. Antimicrobial and human cancer cell cytotoxic effect of synthetic angiotensin-converting enzyme (ACE) inhibitory peptides. Food Chem. 2008, 107, 327-36. DOI: 10.1016/j.foodchem.2007.08.036
Other literature(s)	N.D
PubDate	2008