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 - DFBPDPIV0229(DPP IV-inhibitory peptide)

DFBP ID	DFBPDPIV0229
Peptide sequence	FAGDDAPR
Type	Native peptide
Peptide/Function name	DPP-IV inhibitory peptide, Anti-diabetic peptide

Function-activity relationship

Main bioactivity	DPP-IV inhibitory activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Phe-Ala-Gly-Asp-Asp-Ala-Pro-Arg

Single-letter amino acid

FAGDDAPR

Peptide length

Peptide mass

Experimental mass	Theoretical mass
847.87 Da	847.86 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.92 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.8875^c

Hydrophilic residue ratio

62.5%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal, Marine
Organism/Source	Antarctic krill
Precursor protein	Defatted Antarctic krill powder
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR2751 ---- Plant proteins ---- Actin-7 Source.2: DFBPPR2763 ---- Plant proteins ---- Actin-1 Source.3: DFBPPR2989 ---- Plant proteins ---- Actin-2 Source.4: DFBPPR3087 ---- Plant proteins ---- Actin-3 Source.5: DFBPPR5283 ---- Plant proteins ---- Actin-3 Source.6: DFBPPR5841 ---- Plant proteins ---- Actin-1 Source.7: DFBPPR6550 ---- Plant proteins ---- Actin-3 Source.8: DFBPPR16188 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.9: DFBPPR16883 ---- Animal proteins ---- Actin, aortic smooth muscle Source.10: DFBPPR17154 ---- Animal proteins ---- Actin, cytoplasmic 2 Source.11: DFBPPR17155 ---- Animal proteins ---- Actin, cytoplasmic 2 Source.12: DFBPPR17514 ---- Animal proteins ---- Actin, alpha skeletal muscle Source.13: DFBPPR17747 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.14: DFBPPR18495 ---- Animal proteins ---- Actin, gamma-enteric smooth muscle Source.15: DFBPPR8884 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.16: DFBPPR10103 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.17: DFBPPR10319 ---- Animal proteins ---- Actin, alpha cardiac muscle 1 Source.18: DFBPPR10338 ---- Animal proteins ---- Actin, alpha skeletal muscle Source.19: DFBPPR10431 ---- Animal proteins ---- Actin, aortic smooth muscle Source.20: DFBPPR10478 ---- Animal proteins ---- Actin, gamma-enteric smooth muscle Source.21: DFBPPR10777 ---- Animal proteins ---- Actin, cytoplasmic type 5 Source.22: DFBPPR10810 ---- Animal proteins ---- Actin, cytoplasmic 2 Source.23: DFBPPR12268 ---- Animal proteins ---- Actin, alpha skeletal muscle Source.24: DFBPPR12556 ---- Animal proteins ---- Actin, aortic smooth muscle Source.25: DFBPPR12700 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.26: DFBPPR12701 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.27: DFBPPR13231 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.28: DFBPPR13769 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.29: DFBPPR13996 ---- Animal proteins ---- Actin, alpha skeletal muscle Source.30: DFBPPR14021 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.31: DFBPPR14143 ---- Marine protein ---- Actin, cytoplasmic 1 Source.32: DFBPPR14935 ---- Microorganism protein ---- Actin Source.33: DFBPPR7844 ---- Plant protein ---- Actin-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

DPP IV-inhibitory activity

(1) The peptide FAGDDAPR exhibited potent Dipeptidyl-peptidase IV (EC 3.4.14.5) inhibition activities with IC₅₀ value of 349.70 ± 3.66 μM.
(2) The FAGDDAPR was identified by LC-MS/MS method, and the molecular models of DPP-IV and this peptide was further constructed by AutoDock Vina software, the results revealed that the inhibition activity of FAGDDAPR was mainly attributed to the formation of strong hydrophobic interactions and hydrogen bonds with amino acids of DPP-IV.

Specific target protein(s)

Specific Target Protein(s):
Dipeptidyl peptidase 4

Taste properties & Structure

Bitterness

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

SMILES

N.D

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Compound protease is composed of three proteases (endonuclease, exonuclease, and flavor protease), which exert the best enzymolysis effect of the enzyme under the condition of neutral pH and temperature of 50°C.

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

Defatted Antarctic krill powder is an economical by-product produced in the production of krill oil and contains high-quality protein, but these products were mainly used as fish feed and had low utility value in the past.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Lang M, Song Y, Li Y, Xiang X, Ni L, Miao J. Purification, identification, and molecular mechanism of DPP-IV inhibitory peptides from defatted Antarctic krill powder. J Food Biochem. 2021 Sep;45(9):e13872. PMID: 34296449 DOI: 10.1111/jfbc.13872
Other literature(s)	N.D
PubDate	2021