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 - DFBPALAM0024(α-Amylase inhibitory peptide)

DFBP ID	DFBPALAM0024
Peptide sequence	PLPLHMLP
Type	Native peptide
Peptide/Function name	α-Amylase inhibitory peptide, Anti-diabetic peptide, PBp4

Function-activity relationship

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

Calculated physicochemical properties

Three-letter amino acid

Pro-Leu-Pro-Leu-His-Met-Leu-Pro

Single-letter amino acid

PLPLHMLP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	917.16 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

7.79 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.6625^c

Hydrophilic residue ratio

87.5%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Pinto bean
Precursor protein	Pinto bean 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

α-Amylase inhibitory activity

The peptide PLPLHMLP showed potent α-amylase (EC 3.2.1.1) inhibitory activity with an IC₅₀ value of 15.80 ± 0.17 μM.

Table 1. A summary of potential binding sites between biologically active Pinto bean peptide (PBp) and human salivary a-amylase using Pepsite 2 server and their p-values.
Peptide	p-values	Active amino acids within the sequence	Bound amino acids on ACE
PBp4	0.000908	Pro1, Leu2, Pro3, Leu4, His5, Met6	Pro44, Trp58, Trp59, Tyr62, Asp96, Val98, Arg195; Asp197, Glu233, His299, Asp300

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)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(C)C)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	Integrated bioinformatics approach
Enzyme(s)/starter culture	By using PEAKS studio, 511 peptide sequences were first shortlisted based on their de novo sequence property and average local confidence (ALC) yield of ≥ 60%.

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 three dimensional structure of human a-amylase (PDB code: 1SMD) was imported from the Protein Data Bank (http://www.rcsb.org/pdb/, accessed on 2nd December 2016).
This new approach (integrated bioinformatics-assisted approach) is strongly proposed to be a highly efficient and cost-effective approach in the field of bioactive peptide discovery.

Database cross-references

DFBP

[D1]	DFBPACEI2021
[D2]	DFBPANOX1062
[D3]	DFBPMUFU0603

[D4]

[D5]

[D6]

[D7]

Reference(s)

Primary literature	Ngoh YY, Gan CY. Identification of Pinto bean peptides with inhibitory effects on α-amylase and angiotensin converting enzyme (ACE) activities using an integrated bioinformatics-assisted approach. Food Chem. 2018 Nov 30;267:124-131. PMID: 29934146 DOI: 10.1016/j.foodchem.2017.04.166
Other literature(s)	N.D
PubDate	2018