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 - DFBPINPE0009(Other bio-peptides)

DFBP ID	DFBPINPE0009
Peptide sequence	EITPEKNPQLR
Type	Native peptide
Peptide/Function name	Fatty acid synthase inhibitor

Function-activity relationship

Main bioactivity	Inhibitor activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Glu-Ile-Thr-Pro-Glu-Lys-Asn-Pro-Gln-Leu-Arg

Single-letter amino acid

EITPEKNPQLR

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1324 Da	1324.49 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

7.06 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-1.6364^c

Hydrophilic residue ratio

36.36%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Soybean
Precursor protein	α subunit of β-conglycinin and β subunit of β-conglycinin
Residue position	f(424–434) and f(258–268)
Precursor protein(s) search	Source.1: DFBPPR4975 ---- Plant proteins ---- Beta-conglycinin beta subunit 1 Source.2: DFBPPR4990 ---- Plant proteins ---- Beta-conglycinin alpha' subunit Source.3: DFBPPR5025 ---- Plant proteins ---- Beta-conglycinin alpha subunit 1 Source.4: DFBPPR5035 ---- Plant proteins ---- Beta-conglycinin beta subunit 2 Source.5: DFBPPR5036 ---- Plant proteins ---- Beta-conglycinin alpha subunit 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

Other bioactive activity	The peptide showed Fatty acid synthase (EC 2.3.1.85) inhibitory activity with the IC₅₀ value of 27 mum.
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])(CCC(=O)O)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CC(=O)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Fatty acid synthase inhibitory peptides were produced from soybean β-conglycinin hydrolysis with alcalase from Bacillus licheniformis.

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

This is the first study to identify fatty acid synthase inhibitory peptides from purified beta-conglycinin hydrolysates and predict their binding modes at the molecular level, leading to their possible use as nutraceuticals.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Martinez-Villaluenga C, Rupasinghe SG, Schuler MA, Gonzalez de Mejia E. Peptides from purified soybean beta-conglycinin inhibit fatty acid synthase by interaction with the thioesterase catalytic domain. FEBS J. 2010 Mar;277(6):1481-93. PMID: 20148945 DOI: 10.1111/j.1742-4658.2010.07577.x
Other literature(s)	N.D
PubDate	2010