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 - DFBPALGL0002(α-Glucosidase inhibitory peptide)

DFBP ID	DFBPALGL0002
Peptide sequence	YYPL
Type	Native peptide
Peptide/Function name	α-Glucosidase inhibitory peptide, Anti-diabetic peptide

Function-activity relationship

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

Calculated physicochemical properties

Three-letter amino acid

Tyr-Tyr-Pro-Leu

Single-letter amino acid

YYPL

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	554.63 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.87 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.1000^c

Hydrophilic residue ratio

50%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal, Fish, Marine
Organism/Source	Sardine
Precursor protein	Muscle protein hydrolyzates
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR1605 ---- Plant proteins ---- Phytochrome B Source.2: DFBPPR1843 ---- Plant proteins ---- Laccase-13 Source.3: DFBPPR1882 ---- Plant proteins ---- Laccase-12 Source.4: DFBPPR2378 ---- Plant proteins ---- Probable sucrose-phosphate synthase 2 Source.5: DFBPPR3626 ---- Plant proteins ---- Acyl transferase 7 Source.6: DFBPPR5074 ---- Plant proteins ---- Phytochrome B Source.7: DFBPPR5095 ---- Plant proteins ---- Superoxide dismutase [Fe], chloroplastic Source.8: DFBPPR5460 ---- Plant proteins ---- Peroxidase 2 Source.9: DFBPPR16000 ---- Animal proteins ---- Zona pellucida sperm-binding protein 3 Source.10: DFBPPR16210 ---- Animal proteins ---- Creatine kinase M-type Source.11: DFBPPR17195 ---- Animal proteins ---- Receptor for retinol uptake STRA6 Source.12: DFBPPR17403 ---- Animal proteins ---- Insulin-degrading enzyme Source.13: DFBPPR17527 ---- Animal proteins ---- Brefeldin A-inhibited guanine nucleotide-exchange protein 1 Source.14: DFBPPR18438 ---- Animal proteins ---- Angiopoietin-related protein 4 Source.15: DFBPPR18827 ---- Animal proteins ---- Creatine kinase M-type Source.16: DFBPPR20545 ---- Animal proteins ---- GPI mannosyltransferase 3 Source.17: DFBPPR21422 ---- Animal proteins ---- DNA polymerase alpha subunit B Source.18: DFBPPR9070 ---- Animal proteins ---- Angiopoietin-related protein 4 Source.19: DFBPPR9483 ---- Animal proteins ---- Creatine kinase M-type Source.20: DFBPPR10547 ---- Animal proteins ---- Creatine kinase M-type Source.21: DFBPPR12558 ---- Animal proteins ---- Creatine kinase M-type Source.22: DFBPPR13205 ---- Animal proteins ---- Collagenase 3 Source.23: DFBPPR14303 ---- Marine protein ---- Phycobilisome rod-core linker polypeptide cpcG Source.24: DFBPPR14890 ---- Microorganism protein ---- Killer toxin subunits alpha/beta Source.25: DFBPPR15064 ---- Microorganism protein ---- Palmitoyltransferase SWF1 Source.26: DFBPPR15104 ---- Microorganism protein ---- COP9 signalosome complex subunit 5 Source.27: DFBPPR15539 ---- Microorganism protein ---- Acyl-coenzyme A oxidase Source.28: DFBPPR7802 ---- Plant protein ---- Phytochrome B
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-Glucosidase (AGH, EC 3.2.1.20). IC₅₀ = 3.7 ± 0.02 mM. Inhibitory activity of YYPL was ca. 140-fold weaker than that of a voglibose, typical commercial therapeutic drug (Matsui et al., 1996) (IC₅₀ = 26 μM, Takeda Medical Co., Osaka, Japan). However, considering that the peptides may be used as a physiologically functional food component, the prophylactic effect in diabetes by food would be substantial, regardless of its lower inhibition. The Lineweaver-Burk plots for the inhibition of AGH showed the peptide inhibited AGH competitively.

Table 1 AGH inhibitory activity of synthetic analogues of the peptide isolated from muscle hydrolyzate ^a
Sequence	IC50 (mM)
Tyr-Tyr-Pro-Leu	3.7 ± 0.02
Tyr-Pro-Leu	3.9 ± 0.02
Pro-Leu	No inhibition
Tyr-Pro	16.8 ± 0.08
Tyr-Pro-Gly	5.0 ± 0.01
Tyr-Pro-Tyr	25.8 ± 0.12

^a The analogue peptides were synthesized on the basis of the sequence of Tyr-Tyr-Pro-Leu isolated from the hydrolyzate.

Specific target protein(s)

Specific Target Protein(s):
Lysosomal alpha-glucosidase

Taste properties & Structure

Bitterness

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

SMILES

N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(C)C)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	The peptide was prepared by digestion with Bacillus licheniformis Alkaline protease.

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

AGH inhibitory studies of Try-Tyr-Pro-Leu and its derivatives demonstrated the importance of the tri-peptide chain length as well as the hydrophobic aromatic amino acid tyrosine at the N-terminus, aliphatic amino acids at the C-terminus, as well as an amide proton from the peptide chain at the middle position of the tri-peptide to develop AGH inhibition activity.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Matsui T, Oki T, Osajima Y. Isolation and identification of peptidic alpha-glucosidase inhibitors derived from sardine muscle hydrolyzate. Z Naturforsch C J Biosci. 1999 Mar-Apr;54(3-4):259-63. PMID: 10408829 DOI: 10.1515/znc-1999-3-417
Other literature(s)	[1] Matsui T, Yoshimoto C, Osajima K, et al. In vitro survey of alpha-glucosidase inhibitory food components.[J]. Journal of the Agricultural Chemical Society of Japan, 1996, 60(12):2019-2022.
PubDate	1999