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 - DFBPHYCP0006(Hypocholesterolemic peptide)

DFBP ID	DFBPHYCP0006
Peptide sequence	IAVPGEVA
Type	Native peptide
Peptide/Function name	Hypocholesterolemic peptide

Function-activity relationship

Main bioactivity	Hypocholesterolemic activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Ile-Ala-Val-Pro-Gly-Glu-Val-Ala

Single-letter amino acid

IAVPGEVA

Peptide length

Peptide mass

Experimental mass	Theoretical mass
755.2 Da	754.87 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.34 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

1.3750^c

Hydrophilic residue ratio

87.5%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Soy protein
Precursor protein	11S-globulin
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

Hypocholesterolemic activity

The hypocholesterolemic effect was determined by analysis of bile-acid binding and the percent inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR, EC 1.1.1.88) in vitro. The lowering of the cholesterol content is explained by bile acids bound to hydrolysate peptides shielding them from reabsorption and stimulating the transformation of cholesterol in blood plasma.
An in vitro test for measuring HMGR inhibition showed that the synthesized peptide IAVPGEVA spossessed hypocholesterinemic properties. According to the results, the IC₅₀ for IAVPGEVA was measured as 123.5 μM ^[1].

Specific target protein(s)

Specific Target Protein(s):
3-hydroxy-3-methylglutaryl coenzyme A reductase

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	No prediction can be made about the peptide bitterness. ^prediction

SMILES

N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(C(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)NCC(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(C)C(=O)O

Preparation method

Mode of preparation	Synthetic peptide
Enzyme(s)/starter culture	11S-Globulin was hydrolyzed by pepsin from a Rhizopus sp..

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	Pak, V.V., Koo, M.S., Kasymova, T.D., Kwon, D.Y. Isolation and Identification of Peptides from Soy 11S-Globulin with Hypocholesterolemic Activity. Chemistry of Natural Compounds. 2005, 41, 710-4. DOI: 10.1007/s10600-006-0017-6
Other literature(s)	[1] V. V. Pak, M. Koo, N. Lee, et al. Structure—Activity Relationships of the Peptide Ile-Ala-Val-Pro and Its Derivatives Revealed Using the Semi-Empirical AM1 Method[J]. chemistry of natural compounds, 2005, 41(4):454-460.
PubDate	2005