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 - DFBPACEI0575(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0575
Peptide sequence	TTMPLW
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide, CEI_αC6^[4]

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	Antihypertensive activity ^[D1], DPP IV-inhibitory activity ^[D2], Immunomodulatory activity ^[D3], Opioid activity ^[D4], Multifunctional activity ^[D5]

Calculated physicochemical properties

Three-letter amino acid

Thr-Thr-Met-Pro-Leu-Trp

Single-letter amino acid

TTMPLW

Peptide length

Peptide mass

Experimental mass	Theoretical mass
748 Da	747.90 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.97 ^c

IC₅₀

51 uM, 12 uM ^[2], 16 μM ^[4]

pIC₅₀

-1.708, -1.079, -1.204

GRAVY

0.3000^c

Hydrophilic residue ratio

66.67%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein, Ficus carica ^[1]
Precursor protein	α_s1-Casein
Residue position	f(194-199)
Precursor protein(s) search	Source.1: DFBPPR7688 ---- Milk proteins ---- Alpha-S1-casein Source.2: DFBPPR7717 ---- Milk proteins ---- Alpha-S1-casein Source.3: DFBPPR8488 ---- Milk proteins ---- Alpha-S1-casein
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

ACE-inhibitory activity	(1) The peptide exhibited potent Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 51 μM. (2) The peptide showed potent ACE-inhibitory activity with an IC₅₀ value of 12 uM ^[2]. (3) The peptide showed potent ACE-inhibitory activity with an IC₅₀ value of 16 uM ^[4].
Specific target protein(s)	Specific Target Protein(s): Angiotensin-converting enzyme

Taste properties & Structure

Bitterness

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

SMILES

N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CCSC)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(=CN2)C1=C2C=CC=C1)C(=O)O

Preparation method

Mode of preparation	Fermentation and enzymatic hydrolysis
Enzyme(s)/starter culture	Whey and casein proteins were fermented with lactic acid bacteria and hydrolysed subsequently by digestive enzymes (pepsin and trypsin).

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]	DFBPANHY0140, DFBPANHY0974
[D2]	DFBPDPIV0188
[D3]	DFBPIMMU0029
[D4]	DFBPOPIO0068
[D5]	DFBPMUFU0137

BIOPEP-UWM

[D6]

3127, 3530, 8172, 9619

APD

[D7]

BioPepDB

[D8]

MBPDB

[D9]

Reference(s)

Primary literature	Pihlanto-Leppälä, A., Rokka, T., Korhonen, H. Angiotensin I Converting Enzyme Inhibitory Peptides Derived from Bovine Milk Proteins. International Dairy Journal. 1998, 8, 325-31. DOI: 10.1016/S0958-6946(98)00048-X
Other literature(s)	[1] Maruyama S, Miyoshi S, Tanaka H. Angiotensin I-Converting Enzyme Inhibitors Derived from Ficus carica[J]. Journal of the Agricultural Chemical Society of Japan, 1989, 53(10):2763-2767. [2] Murray B A, Fitzgerald R J. Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production[J]. Current Pharmaceutical Design, 2007, 13(8):-. [3] Bösze Z. Bioactive Components of Milk[M]. Springer New York, 2008. [4] Maruyama S, Mitachi H, Awaya J, et al. Angiotensin I-Converting Enzyme Inhibitory Activity of the C-Terminal Hexapeptide of αs1-Casein[J]. Agricultural and biological chemistry, 1987, 51(9):2557-2561. [5] Tauzin, J., L. Miclo, and J.L. Gaillard, Angiotensin-I-converting enzyme inhibitory peptides from tryptic hydrolysate of bovine alphaS2-casein. FEBS Lett, 2002. 531(2): p. 369-74. [6] De Gobba, C., G. Tompa, and J. Otte, Bioactive peptides from caseins released by cold active proteolytic enzymes from Arsukibacterium ikkense. Food Chem, 2014. 165: p. 205-15.
PubDate	1998