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 - DFBPANOX1059(Antioxidative peptide)

DFBP ID	DFBPANOX1059
Peptide sequence	PPHMLP
Type	Native peptide
Peptide/Function name	Antioxidative peptide

Function-activity relationship

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

Calculated physicochemical properties

Three-letter amino acid

Pro-Pro-His-Met-Leu-Pro

Single-letter amino acid

PPHMLP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
690.35 Da	690.85 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

7.79 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.3833^c

Hydrophilic residue ratio

83.33%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Pinto beans (Phaseolus vulgaris cv. Pinto)
Precursor protein	Pinto beans protein
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

Antioxidative activity

Peptide fraction < 3 kDa, which exhibited the highest antioxidant activities (i.e., ABTS (42.2%) and FRAP (0.81mM)) and α-amylase inhibitory activity (62.1%), was then subjected to LCMS and MS/MS analyses. Six sequences (PPHMLP, PPMHLP, PLPPHMLP, PLPLHMLP, ACSNHSPLGWRGH, LSSLEMGSLGALFVCM) were identified for antioxidant peptides, whereas seven (PPHMLP, PPMHLP, PLPWGAGF, GDAACCGLPLLP, PPHMGGP, PLPPHDLL, FNPFPSPHTP) peptides for α-amylase inhibitor. These peptide sequences were suggested to be the potential contributor to both antioxidant and α-amylase inhibitory activity (Synthetic peptide was not tested).

Specific target protein(s)

N.D

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Bitter taste ^prediction

SMILES

N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])(CCSC)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	The highest antioxidant and α-amylase inhibitor peptides derived from pinto bean protein isolate was obtained from pH 7.5 and pH 6.5, respectively, under the condition of extraction time of 1 h with a S/E ratio of 10 at 50 ℃.

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]	DFBPACEI2018
[D2]	DFBPALAM0021, DFBPALAM0029
[D3]	DFBPMUFU0600

[D4]

[D5]

[D6]

[D7]

Reference(s)

Primary literature	Ngoh YY, Gan CY. Enzyme-assisted extraction and identification of antioxidative and α-amylase inhibitory peptides from Pinto beans (Phaseolus vulgaris cv. Pinto). Food Chem. 2016 Jan 1;190:331-337. PMID: 26212978 DOI: 10.1016/j.foodchem.2015.05.120
Other literature(s)	N.D
PubDate	2016