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List of peptide properties
DFBP ID - DFBPMIBP0019(Mineral-binding peptide)
DFBP ID DFBPMIBP0019
Peptide sequence VYQHQKAMKPWIQPKTKVIPYVRY
Type Native peptide
Peptide/Function name Mineral-binding petpide, Calmodulin-binding peptide
Function-activity relationship
Main bioactivity Mineral-binding activity
Otheir bioactivity Antimicrobial activity [D1], Haemolytic activity [D2], Multifunctional activity [D3]
Calculated physicochemical properties
Three-letter amino acid Val-Tyr-Gln-His-Gln-Lys-Ala-Met-Lys-Pro-Trp-Ile-Gln-Pro-Lys-Thr-Lys-Val-Ile-Pro-Tyr-Val-Arg-Tyr
Single-letter amino acid VYQHQKAMKPWIQPKTKVIPYVRY
Peptide length 24
Peptide mass
Experimental mass Theoretical mass
N.D 3002.62 Da c
Net charge 0.00 c
Isoelectric point (pI) 10.48 c
IC50 N.D
pIC50 N.D
GRAVY -0.7833 c
Hydrophilic residue ratio 45.83% 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 αs2-Casein
Residue position f(183-206)
Precursor protein(s) search
Link-research
There are no literature reports on the discovery of this sequence in other food-source proteins.
Biological/Functional activity & target protein
Mineral-binding activity

Fig. 1 shows the effects of αs2-casein (164-179), αs2-casein (183-206) and αs2-casein (183-207) on Calmodulin-induced activation of 3',5'-cyclic-nucleotide phosphodiesterase (PDE, EC 3.1.4.17). The approximate IC50 values of these peptides were 38, 6.9 and 1.1 μM respectively. The concentration of each peptide that totally inhibited the activation of PDE induced by Calmodulin had no significant effect on the basal PDE activity.

1995.png
Fig. 1. Effects of the peptides derived from α-casein on the calmodulin-indueed phosphodiesterase activation. Effects of various concentrations of ○, αs2-casein (164-179); △, αs2-casein (183-206) and □, αs2-casein (183-207) are shown. Each point is the mean of duplicate determinations.
Specific target protein(s) Specific Target Protein(s):
3',5'-cyclic-nucleotide phosphodiesterase
Taste properties & Structure
Bitterness
Literature report N.D
Bitter prediction tools Bitter taste prediction
SMILES N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CCSC)C(=O)N[C@@]([H])(CCCCN)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(=CN2)C1=C2C=CC=C1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)O
Preparation method
Mode of preparation

Enzymatic hydrolysis

Enzyme(s)/starter culture

Peptides that inhibit calmodulin-dependent cyclic nucleotide phosphodiesterase were isolated from a pepsin digest of α-casein.

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

These results demonstrated that the affinities of these peptides for calmodulin are comparable to the affinities of certain endogenous neurohormones and proteins that interact with calmodulin.

Database cross-references
DFBP
[D1] DFBPAMIC0282
[D2] DFBPHAPE0020
[D3] DFBPMUFU0706
BIOPEP-UWM [D4] 3033, 3435, 3965
APD [D5] -
BioPepDB [D6] -
MBPDB [D7] -
Reference(s)
Primary literature Kizawa K, Naganuma K, Murakami U. Calmodulin-binding peptides isolated from alpha-casein peptone. J Dairy Res. 1995 Nov;62(4):587-92.
PMID: 8568029
Other literature(s) N.D
PubDate 1995
Copyright © 2020. Record / license number: Chongqing ICP No. 2000214