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 - DFBPALAM0025(α-Amylase inhibitory peptide)

DFBP ID	DFBPALAM0025
Peptide sequence	LSSLEMGSLGALFVCM
Type	Native peptide
Peptide/Function name	α-Amylase inhibitory peptide, Anti-diabetic peptide, PBp5

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

Leu-Ser-Ser-Leu-Glu-Met-Gly-Ser-Leu-Gly-Ala-Leu-Phe-Val-Cys-Met

Single-letter amino acid

LSSLEMGSLGALFVCM

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1658.00 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.34 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

1.4750^c

Hydrophilic residue ratio

68.75%^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 LSSLEMGSLGALFVCM showed potent α-amylase (EC 3.2.1.1) inhibitory activity with an IC₅₀ value of 10.03 ± 0.47 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
PBp5	0.020210, 0.006123	Leu1, Ser2, Ser3, Leu4, Met6, Ser8, Ala11, Leu12, Phe13, Val14, Cys15, Met16	Phe17, Gln41, Pro44, Trp58, Trp59, Tyr62, Asp96, Val98, Arg195, Asp197, Glu233, Asn298, His299, Asp300, His305, Lys352, Asp356

Specific target protein(s)

N.D

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Non-bitter taste ^prediction

SMILES

N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CCSC)C(=O)NCC(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CC(C)C)C(=O)NCC(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(CCSC)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]	DFBPACEI2022
[D2]	DFBPANOX1064
[D3]	DFBPMUFU0604

[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