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 - DFBPAMIC0338(Antimicrobial peptide)

DFBP ID	DFBPAMIC0338
Peptide sequence	IPAVFK
Type	Native peptide
Peptide/Function name	Antibacterial peptide

Function-activity relationship

Main bioactivity	Antimicrobial activity
Otheir bioactivity	ACE-inhibitory activity ^[D1], Antioxidative activity ^[D2], DPP IV-inhibitory activity ^[D3], Multifunctional activity ^[D4]

Calculated physicochemical properties

Three-letter amino acid

Ile-Pro-Ala-Val-Phe-Lys

Single-letter amino acid

IPAVFK

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	673.84 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

10.04 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

1.3000^c

Hydrophilic residue ratio

83.33%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bos taurus (Bovine)
Precursor protein	β-Lactoglobulin
Residue position	f(78-83)
Precursor protein(s) search	Source.1: DFBPPR0115 ---- Milk proteins ---- Beta-lactoglobulin Source.2: DFBPPR7687 ---- Milk proteins ---- Beta-lactoglobulin Source.3: DFBPPR7698 ---- Milk proteins ---- Beta-lactoglobulin-1/B Source.4: DFBPPR7714 ---- Milk proteins ---- Beta-lactoglobulin Source.5: DFBPPR8499 ---- Milk proteins ---- Beta-lactoglobulin
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	The peptide showed bactericidal activity against several gram-positive bacteria.
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@]([H])(CC)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CCCCN)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Peptide obtained by hydrolysis of β-lactoglobulin by use of trypsin.

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]	DFBPACEI0645
[D2]	DFBPANOX0700
[D3]	DFBPDPIV0046
[D4]	DFBPMUFU0443

BIOPEP-UWM

[D5]

8196, 8621, 9232

APD

[D6]

BioPepDB

[D7]

MBPDB

[D8]

Reference(s)

Primary literature	Pellegrini A, Dettling C, Thomas U, Hunziker P. Isolation and characterization of four bactericidal domains in the bovine beta-lactoglobulin. Biochim Biophys Acta. 2001 May 3;1526(2):131-40. PMID: 11325534 DOI: 10.1016/s0304-4165(01)00116-7
Other literature(s)	[1] Power O, Fernández A, Norris R, et al. Selective enrichment of bioactive properties during ultrafiltration of a tryptic digest of β-lactoglobulin[J]. Journal of Functional Foods, 2014, 9:38-47.
PubDate	2001