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 - DFBPAMIC0198(Antimicrobial peptide)

DFBP ID	DFBPAMIC0198
Peptide sequence	YQEPVLGPVRGPFPIIV
Type	Native peptide
Peptide/Function name	Antimicrobial peptide

Function-activity relationship

Main bioactivity	Antimicrobial activity
Otheir bioactivity	ACE-inhibitory activity ^[D1], Antihypertensive activity ^[D2], Antithrombotic activity ^[D3], Immunomodulatory activity ^[D4], Multifunctional activity ^[D5]

Calculated physicochemical properties

Three-letter amino acid

Tyr-Gln-Glu-Pro-Val-Leu-Gly-Pro-Val-Arg-Gly-Pro-Phe-Pro-Ile-Ile-Val

Single-letter amino acid

YQEPVLGPVRGPFPIIV

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1881.24 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

6.88 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.4824^c

Hydrophilic residue ratio

76.47%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Casein
Precursor protein	β-Casein
Residue position	f(193-209)
Precursor protein(s) search	Source.1: DFBPPR7718 ---- Milk proteins ---- Beta-casein Source.2: DFBPPR8489 ---- Milk proteins ---- Beta-casein
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	Anti-Gram-; Active against E. coli DH5a, E. coli DPC6053 and E. sakazakii (MIC 0.2 to >1.0 mg/ml).
Specific target protein(s)	N.D

Taste properties & Structure

Bitterness

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

SMILES

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

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Hydrolysis with Trypsin or Chymosin.

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

DFBP

[D1]	DFBPACEI0427, DFBPACEI1401
[D2]	DFBPANHY0117
[D3]	DFBPANTH0103
[D4]	DFBPIMMU0033
[D5]	DFBPMUFU0119

[D6]

[D7]

[D8]

[D9]

Reference(s)

Primary literature	Birkemo GA, O'Sullivan O, Ross RP, Hill C. Antimicrobial activity of two peptides casecidin 15 and 17, found naturally in bovine colostrum. J Appl Microbiol. 2009 Jan;106(1):233-40. PMID: 19054235 DOI: 10.1111/j.1365-2672.2008.03996.x
Other literature(s)	[1] Park Y W. Bioactive Components in Milk and Dairy Products[M]. 2009. [2] Sandre, C., et al., A peptide derived from bovine beta-casein modulates functional properties of bone marrow-derived macrophages from germfree and human flora-associated mice. J Nutr, 2001. 131(11): p. 2936-42. [3] Rojas-Ronquillo R , Cruz-Guerrero A , Angélica Flores-Nájera, et al. Antithrombotic and angiotensin-converting enzyme inhibitory properties of peptides released from bovine casein by Lactobacillus casei Shirota[J]. International Dairy Journal, 2012, 26(2). [4] Hayes, M., et al., Casein fermentate of Lactobacillus animalis DPC6134 contains a range of novel propeptide angiotensin-converting enzyme inhibitors. Appl Environ Microbiol, 2007. 73(14): p. 4658-67.
PubDate	2009