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 - DFBPALGL0024(α-Glucosidase inhibitory peptide)

DFBP ID	DFBPALGL0024
Peptide sequence	FFRSKLLSDGAAAAKGALLPQYW
Type	Native peptide
Peptide/Function name	α-Glucosidase inhibitory peptide, Anti-diabetic peptide, CSP1

Function-activity relationship

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

Calculated physicochemical properties

Three-letter amino acid

Phe-Phe-Arg-Ser-Lys-Leu-Leu-Ser-Asp-Gly-Ala-Ala-Ala-Ala-Lys-Gly-Ala-Leu-Leu-Pro-Gln-Tyr-Trp

Single-letter amino acid

FFRSKLLSDGAAAAKGALLPQYW

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	2510.87 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

10.18 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.1870^c

Hydrophilic residue ratio

65.22%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Cumin (Cuminum cyminum)
Precursor protein	Seed 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-Glucosidase inhibitory activity	Inhibitor of α-amylase (EC 3.2.1.1). In terms of amylase inhibitory activity for 100 μg of the purified peptide, CSP1 exhibited the strongest inhibitory action against porcine pancreatic α-amylase (PPA), with an observed inhibitory activity of 24.54% and an IC₅₀ value of 0.02 μM.
Specific target protein(s)	Specific Target Protein(s): Lysosomal alpha-glucosidase

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])(Cc1ccccc1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CC(=O)O)C(=O)NCC(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CCCCN)C(=O)NCC(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CC(=CN2)C1=C2C=CC=C1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Cumin seed protein isolate (CSPI) was enzymatically hydrolyzed using Protamex under the optimum condition.

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

Bioactive peptides derived from cumin seeds potentially contribute to the management of diabetes because of their ability to inhibit enzymes related to glucose absorption. Hence, the anti-amylase properties of peptides from cumin seeds can further increase its nutritional values in addition to their future applications.

Database cross-references

DFBP

[D1]	DFBPANOX0539
[D2]	DFBPALAM0001
[D3]	DFBPMUFU0665

[D4]

[D5]

[D6]

[D7]

Reference(s)

Primary literature	Siow, H.-L., Gan, C.-Y. Extraction, identification, and structure–activity relationship of antioxidative and α-amylase inhibitory peptides from cumin seeds (Cuminum cyminum). Journal of Functional Foods. 2016, 22, 1-12. DOI: 10.1016/j.jff.2016.01.011
Other literature(s)	N.D
PubDate	2016