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 - DFBPACEI0123(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0123
Peptide sequence	VECYGPNRPQF
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

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

Calculated physicochemical properties

Three-letter amino acid

Val-Glu-Cys-Tyr-Gly-Pro-Asn-Arg-Pro-Gln-Phe

Single-letter amino acid

VECYGPNRPQF

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1309 Da	1309.47 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

6.29 ^c

IC₅₀

29.6 uM

pIC₅₀

-1.471

GRAVY

-0.9455^c

Hydrophilic residue ratio

45.45%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant, Algae
Organism/Source	Microalgae, Chlorella vulgaris
Precursor protein	Algae protein waste 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

ACE-inhibitory activity	The peptide exhibited potent Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 29.6 μM, and its ACE inhibitory pattern was shown by Lineweaver–Burk plots to be a non-competitive inhibition pattern.
Specific target protein(s)	Specific Target Protein(s): Angiotensin-converting enzyme

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

Structure

Embedded Mol* Viewer

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Docking

Embedded Mol* Viewer

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Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Algae protein waste was hydrolyzed with Pepsin.

Stability & Cytotoxicity

Peptide stability

Literature report:	The purified hendeca-peptide completely retained its ACE inhibitory activity at a pH range of 2–10, temperatures of 40–100 °C, as well as after treatments in vitro by a gastrointestinal enzyme, thus indicating its heat- and pH-stability.
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	N.D
Prediction:	ToxinPred

Additional information

(1) Algae protein waste is a by-product during production of algae essence from Chlorella vulgaris.
(2) The combination of the biochemical properties of this isolated hendeca-peptide and a cheap algae protein resource make an attractive alternative for producing a high value product for blood pressure regulation as well as water and fluid balance.

Database cross-references

DFBP

[D1]	DFBPANOX0166
[D2]	DFBPANCA0009
[D3]	DFBPMUFU0052

BIOPEP-UWM

[D4]

8137, 8138, 8997

APD

[D5]

BioPepDB

[D6]

MBPDB

[D7]

Reference(s)

Primary literature	Sheih, I.C., Fang, T.J., Wu, T.-K. Isolation and characterisation of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from the algae protein waste. Food Chem. 2009, 115, 279-84. DOI: 10.1016/j.foodchem.2008.12.019
Other literature(s)	[1] Sheih I C, Fang T J, Wu T K, et al. Anticancer and antioxidant activities of the peptide fraction from algae protein waste.[J]. Journal of Agricultural & Food Chemistry, 2010, 58(2):1202-7. [2] Sheih I C, Wu T K, Fang T J. Antioxidant properties of a new antioxidative peptide from algae protein waste hydrolysate in different oxidation systems.[J]. Bioresource Technology, 2009, 100(13):3419.
PubDate	2009