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 - DFBPALAM0039(α-Amylase inhibitory peptide)

DFBP ID	DFBPALAM0039
Peptide sequence	SPFWNINAH
Type	Native peptide
Peptide/Function name	α-Amylase inhibitory peptide, Anti-diabetic peptide, P3

Function-activity relationship

Main bioactivity	α-Amylase inhibitory activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Ser-Pro-Phe-Trp-Asn-Ile-Asn-Ala-His

Single-letter amino acid

SPFWNINAH

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1085.18 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

7.79 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.4889^c

Hydrophilic residue ratio

55.56%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Oat
Precursor protein	Oat bran proteins
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR1702 ---- Plant proteins ---- Glutelin type-A 2 Source.2: DFBPPR2035 ---- Plant proteins ---- Glutelin type-A 1 Source.3: DFBPPR2151 ---- Plant proteins ---- Glutelin type-A 3 Source.4: DFBPPR2914 ---- Plant proteins ---- Glutelin type-D 1
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 maximum inhibition of SPFWNINAH for α-amylase was 18% at 133.3 μM, and as such, its IC₅₀ could not be determined.
Specific target protein(s)	N.D

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	No prediction can be made about the peptide bitterness. ^prediction

SMILES

N.D

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Oat bran proteins were hydrolyzed with either the papain or protamex.

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

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Esfandi R, Seidu I, Willmore W, Tsopmo A. Antioxidant, pancreatic lipase, and α-amylase inhibitory properties of oat bran hydrolyzed proteins and peptides. J Food Biochem. 2021 May 16:e13762. PMID: 33997997 DOI: 10.1111/jfbc.13762
Other literature(s)	N.D
PubDate	2021