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 - DFBPACEI1293(ACE-inhibitory peptide)

DFBP ID	DFBPACEI1293
Peptide sequence	LEEAF
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

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

Calculated physicochemical properties

Three-letter amino acid

Leu-Glu-Glu-Ala-Phe

Single-letter amino acid

LEEAF

Peptide length

Peptide mass

Experimental mass	Theoretical mass
607.3 Da	607.65 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.19 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.2800^c

Hydrophilic residue ratio

60%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Hemp (Cannabis sativa L.)
Precursor protein	Hemp seed protein
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR1595 ---- Plant proteins ---- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B Source.2: DFBPPR5932 ---- Plant proteins ---- Probable glutathione S-transferase BZ2 Source.3: DFBPPR7098 ---- Plant proteins ---- Acyl carrier protein 2, chloroplastic Source.4: DFBPPR7220 ---- Plant proteins ---- Chalcone synthase 1 Source.5: DFBPPR8186 ---- Plant proteins ---- 11S globulin subunit beta Source.6: DFBPPR15942 ---- Animal proteins ---- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B Source.7: DFBPPR19772 ---- Animal proteins ---- ADP-dependent glucokinase Source.8: DFBPPR20656 ---- Animal proteins ---- Protein archease Source.9: DFBPPR8992 ---- Animal proteins ---- Hyaluronidase-3 Source.10: DFBPPR11626 ---- Animal proteins ---- tRNA-splicing endonuclease subunit Sen2 Source.11: DFBPPR11740 ---- Animal proteins ---- 55 kDa erythrocyte membrane protein Source.12: DFBPPR7838 ---- Plant protein ---- Chalcone synthase 6 Source.13: DFBPPR7839 ---- Plant protein ---- Chalcone synthase 7 Source.14: DFBPPR7840 ---- Plant protein ---- Chalcone synthase 1 Source.15: DFBPPR7841 ---- Plant protein ---- Chalcone synthase 4 Source.16: DFBPPR7842 ---- Plant protein ---- Chalcone synthase 3 Source.17: DFBPPR7845 ---- Plant protein ---- Chalcone synthase 5 Source.18: DFBPPR7848 ---- Plant protein ---- Chalcone synthase 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

ACE-inhibitory activity	The peptide exhibited 35% Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibition.
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])(CC(C)C)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Hemp seed proteins was hydrolyzed by simulating gastrointestinal tract digestion (Pepsin and Pancreatin).

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

The peptide showed 42% renin inhibition.

Database cross-references

DFBP

[D1]	DFBPANOX0652
[D2]	DFBPMUFU0300

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Girgih, A.T., He, R., Malomo, S., Offengenden, M., Wu, J., Aluko, R.E. Structural and functional characterization of hemp seed (Cannabis sativa L.) protein-derived antioxidant and antihypertensive peptides. Journal of Functional Foods. 2014, 6, 384-94. DOI: 10.1016/j.jff.2013.11.005
Other literature(s)	N.D
PubDate	2014