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List of peptide properties
DFBP ID - DFBPACEI0419(ACE-inhibitory peptide)
DFBP ID DFBPACEI0419
Peptide sequence HLPLP
Type Native peptide
Peptide/Function name ACE-inhibitory peptide
Function-activity relationship
Main bioactivity ACE-inhibitory activity
Otheir bioactivity Antihypertensive activity [D1], Antioxidative activity [D2], Multifunctional activity [D3]
Calculated physicochemical properties
Three-letter amino acid His-Leu-Pro-Leu-Pro
Single-letter amino acid HLPLP
Peptide length 5
Peptide mass
Experimental mass Theoretical mass
576.3 Da 575.70 Da c
Net charge 0.00 c
Isoelectric point (pI) 7.79 c
IC50 41 μM, 21 uM [2]
pIC50 -1.613, -1.322
GRAVY 0.2400 c
Hydrophilic residue ratio 80% c
Peptide calculator
To calculate the physicochemical properties of bioactive peptide.
Peptide source & Food-borne protein(s) search
Classification Animal
Organism/Source Milk protein
Precursor protein β-Casein
Residue position

f(149-153)

Precursor protein(s) search
Source.1: DFBPPR1798 ---- Plant proteins ---- UMP-CMP kinase 2
Source.2: DFBPPR3187 ---- Plant proteins ---- Probable glucuronosyltransferase Os10g0205300
Source.3: DFBPPR4827 ---- Plant proteins ---- BURP domain-containing protein 1
Source.4: DFBPPR7605 ---- Milk proteins ---- Beta-casein
Source.5: DFBPPR7665 ---- Milk proteins ---- Beta-casein
Source.6: DFBPPR7692 ---- Milk proteins ---- Beta-casein
Source.7: DFBPPR7700 ---- Milk proteins ---- Beta-casein
Source.8: DFBPPR7718 ---- Milk proteins ---- Beta-casein
Source.9: DFBPPR8489 ---- Milk proteins ---- Beta-casein
Source.10: DFBPPR16229 ---- Animal proteins ---- 5-hydroxytryptamine receptor 1A
Source.11: DFBPPR16270 ---- Animal proteins ---- AP-4 complex subunit mu-1
Source.12: DFBPPR17683 ---- Animal proteins ---- Cyanocobalamin reductase / alkylcobalamin dealkylase
Source.13: DFBPPR19085 ---- Animal proteins ---- AP-4 complex subunit mu-1
Source.14: DFBPPR21483 ---- Animal proteins ---- F-box/LRR-repeat protein 8
Source.15: DFBPPR13225 ---- Animal proteins ---- 5-hydroxytryptamine receptor 1A
Source.16: DFBPPR15017 ---- Microorganism protein ---- Serine/threonine-protein kinase TEL1
Link-research
Link 1: DFBPACEI0418----Human milk protein----β-Casein
Biological/Functional activity & target protein
ACE-inhibitory activity

The peptide exhibited potent Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC50 value of 41 μM.

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])(CC1=CN=C-N1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)O
Preparation method
Mode of preparation

Fermentation

Enzyme(s)/starter culture

Milk proteins was fermented with Lactobacillus (Lb.) helveticus NCC 2765.

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
Additional information N.D
Database cross-references
DFBP
[D1] DFBPANHY0003
[D2] DFBPANOX0710
[D3] DFBPMUFU0116
BIOPEP-UWM [D4] 2666
APD [D5] -
BioPepDB [D6] -
MBPDB [D7] -
Reference(s)
Primary literature Robert MC, Razaname A, Mutter M, Juillerat MA. Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765. J Agric Food Chem. 2004 Nov 17;52(23):6923-31.
PMID: 15537298
Other literature(s)

[1] Kohmura M, Nio N, Kubo K, et al. Inhibition of angiotensin-converting enzyme by synthetic peptides of human. BETA.-casein[J]. Journal of the Agricultural Chemical Society of Japan, 1989, 53(8):2107-2114.
[2] Hernandezledesma B, Quiros A, Amigo L, et al. Identification of bioactive peptides after digestion of human milk and infant formula with pepsin and pancreatin[J]. International Dairy Journal, 2007, 17(1):42-49.
[3] Sánchez-Rivera L, Santos P F, Miralles B, et al. Peptide fragments from β-casein f(134–138), HLPLP, generated by the action of rat blood plasma peptidases show potent antihypertensive activity[J]. Food Research International, 2016, 88:348-353.

PubDate 2004
Copyright © 2020. Record / license number: Chongqing ICP No. 2000214