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 - DFBPDPIV0124(DPP IV-inhibitory peptide)

DFBP ID	DFBPDPIV0124
Peptide sequence	MPPPLPA
Type	Native peptide
Peptide/Function name	DPP-IV inhibitory peptide, Anti-diabetic peptide

Function-activity relationship

Main bioactivity	DPP-IV inhibitory activity
Otheir bioactivity	PEP-inhibitory activity ^[D1], Multifunctional activity ^[D2]

Calculated physicochemical properties

Three-letter amino acid

Met-Pro-Pro-Pro-Leu-Pro-Ala

Single-letter amino acid

MPPPLPA

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	721.90 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.97 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.1571^c

Hydrophilic residue ratio

100%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine brain
Precursor protein	Glial fibrillary acidic protein (GFAP)
Residue position	f(38-44)
Precursor protein(s) search	Source.1: DFBPPR19635 ---- Animal proteins ---- Glial fibrillary acidic protein
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	This peptide showed Dipeptidyl Peptidase IV (EC 3.4.14.5) inhibitory activity with the IC₅₀ values of 1300 uM and it's weakly active.
Specific target protein(s)	Specific Target Protein(s): Dipeptidyl peptidase 4

Taste properties & Structure

Bitterness

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

SMILES

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

Preparation method

Mode of preparation	Chmical synthesis
Enzyme(s)/starter culture	The peptide was synthesized by the solid phase method with a 430A Peptide Synthesizer (Applied Biosystems. Inc.).

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

DFBP

[D1]	DFBPPEPI0037
[D2]	DFBPMUFU0730

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Maruyama S, Ohmori T, Nakagami T. Prolylendopeptidase inhibitory activity of a glial fibrillary acidic protein fragment and other proline-rich peptides. Biosci Biotechnol Biochem. 1996 Feb;60(2):358-9. PMID: 9063991 DOI: 10.1271/bbb.60.358
Other literature(s)	N.D
PubDate	1996