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 - DFBPANHY0140(Antihypertensive peptide)

DFBP ID	DFBPANHY0140
Peptide sequence	TTMPLW
Type	Native peptide
Peptide/Function name	Antihypertensive peptide

Function-activity relationship

Main bioactivity	Antihypertensive activity
Otheir bioactivity	ACE-inhibitory 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

N.D

pIC₅₀

N.D

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
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	Link 1: DFBPANHY0974----Milk protein----α_s1-Casein

Biological/Functional activity & target protein

Antihypertensive activity	This hexapeptide TTMPLW, when intravenously administered to anesthetized rats at 31.8 mg/kg, tended to antagonize the rats' pressor response to angiotensin I.
Specific target protein(s)	N.D

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	Synthesis
Enzyme(s)/starter culture	The chemical synthesis of peptides was carried out by the liquid phase method, using N,N-dimethylformamide as a solvent with N,N'-dicyclohexylcarbodiimide and 1-hydroxybenzotriazole as coupling reagents.

Stability & Cytotoxicity

Peptide stability

Literature report:	N.D
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	Non-Toxin
Prediction:	ToxinPred

Additional information

N.D

Database cross-references

DFBP

[D1]	DFBPACEI0575
[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	Maruyama, S., Mitachi, H., Awaya, J., Kurono, M., Tomizuka, N., Suzuki, H. Angiotensin I-Converting Enzyme Inhibitory Activity of the C-Terminal Hexapeptide of αs1-Casein. Agricultural and Biological Chemistry. 2016, 51, 2557-61. DOI: 10.1080/00021369.1987.10868415
Other literature(s)	[1] Park Y W. Bioactive Components in Milk and Dairy Products[M]. 2009. [2] Maruyama S, Suzuki H. A Peptide Inhibitor of Angiotensin I Converting Enzyme in the Tryptic Hydrolysate of Casein[J]. Journal of the Agricultural Chemical Society of Japan, 1982, 46(5):1393-1394. [3] Pihlanto-Leppala, A., T. Rokka, and H. Korhonen, Angiotensin I converting enzyme inhibitory peptides derived from bovine milk proteins. International Dairy Journal, 1998. 8(4): p. 325-331. [4] Ha, G.E., et al., Identification of Antihypertensive Peptides Derived from Low Molecular Weight Casein Hydrolysates Generated during Fermentation by Bifidobacterium longum KACC 91563. Korean J Food Sci Anim Resour, 2015. 35(6): p. 738-747.
PubDate	2016