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 - DFBPANOX0028(Antioxidative peptide)

DFBP ID	DFBPANOX0028
Peptide sequence	HLHP
Type	Native peptide
Peptide/Function name	Antioxidative peptide

Function-activity relationship

Main bioactivity	Antioxidative activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

His-Leu-His-Pro

Single-letter amino acid

HLHP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	502.57 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

7.95 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-1.0500^c

Hydrophilic residue ratio

50%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Designed peptide
Organism/Source	Designed peptide
Precursor protein	Designed peptide based on the antioxidative peptide: LLPHH
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR1062 ---- Plant proteins ---- Transcription factor LAX PANICLE 1 Source.2: DFBPPR2736 ---- Plant proteins ---- Ethylene-responsive transcription factor ABI4 Source.3: DFBPPR2753 ---- Plant proteins ---- Transportin-1 Source.4: DFBPPR2924 ---- Plant proteins ---- Probable glycosyltransferase 7 Source.5: DFBPPR3267 ---- Plant proteins ---- CDP-diacylglycerol--serine O-phosphatidyltransferase 3 Source.6: DFBPPR3534 ---- Plant proteins ---- Cardiolipin synthase (CMP-forming), mitochondrial Source.7: DFBPPR3673 ---- Plant proteins ---- Zinc-finger homeodomain protein 3 Source.8: DFBPPR4307 ---- Plant proteins ---- Acyl transferase 8 Source.9: DFBPPR4655 ---- Plant proteins ---- Zinc finger CCCH domain-containing protein 7 Source.10: DFBPPR4861 ---- Plant proteins ---- B3 domain-containing protein Os06g0112300 Source.11: DFBPPR5833 ---- Plant proteins ---- O-methyltransferase ZRP4 Source.12: DFBPPR6316 ---- Plant proteins ---- Protein TIC 20, chloroplastic Source.13: DFBPPR8206 ---- Plant proteins ---- DELLA protein GAIP-B Source.14: DFBPPR15979 ---- Animal proteins ---- Serine/threonine-protein kinase NLK Source.15: DFBPPR17395 ---- Animal proteins ---- Ubiquitin carboxyl-terminal hydrolase CYLD Source.16: DFBPPR17459 ---- Animal proteins ---- Beta-1,4-galactosyltransferase 3 Source.17: DFBPPR18320 ---- Animal proteins ---- Serine/threonine-protein kinase NLK Source.18: DFBPPR18654 ---- Animal proteins ---- SMC5-SMC6 complex localization factor protein 1 Source.19: DFBPPR19240 ---- Animal proteins ---- Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial Source.20: DFBPPR19301 ---- Animal proteins ---- E3 ubiquitin-protein ligase RNF220 Source.21: DFBPPR19399 ---- Animal proteins ---- UBX domain-containing protein 6 Source.22: DFBPPR19532 ---- Animal proteins ---- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16 Source.23: DFBPPR20451 ---- Animal proteins ---- Alpha-(1,3)-fucosyltransferase 10 Source.24: DFBPPR20523 ---- Animal proteins ---- Vacuolar protein-sorting-associated protein 36 Source.25: DFBPPR21221 ---- Animal proteins ---- Short-chain dehydrogenase/reductase family 42E member 1 Source.26: DFBPPR21835 ---- Animal proteins ---- Protein misato homolog 1 Source.27: DFBPPR8992 ---- Animal proteins ---- Hyaluronidase-3 Source.28: DFBPPR10275 ---- Animal proteins ---- Bone morphogenetic protein receptor type-1B Source.29: DFBPPR10318 ---- Animal proteins ---- LIM domain kinase 1 Source.30: DFBPPR10990 ---- Animal proteins ---- Period circadian protein homolog 2 Source.31: DFBPPR11131 ---- Animal proteins ---- Phenylalanine--tRNA ligase alpha subunit Source.32: DFBPPR11264 ---- Animal proteins ---- Charged multivesicular body protein 7 Source.33: DFBPPR13929 ---- Animal proteins ---- Homeobox protein Hox-A4 Source.34: DFBPPR15243 ---- Microorganism protein ---- Coupling of ubiquitin conjugation to ER degradation protein 1
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

Antioxidative activity

The peptide HLHP was designed based on an antioxidative peptide (Leu-Leu-Pro-His-His) derived from proteolytic digests of a soybean protein. It showed potent antioxidative activity, as shown in Table 1.

Table 1. Synergistic Effects of Synthetic Peptides on the Antioxidative Activity of Nonpeptidic Antioxidants ^a
	Antioxidative activity
	peptide	+BHA	+BHT	+tocopherol
Antioxidant
	1.0
BHA		2.4
BHT			1.9
tocopherol				1.3
Synthetic Peptide
HPLH	0.6	13.1 (4.4)	5.7 (2.3)	7.2 (3.8)
HHLP	0.9	16.1 (4.9)	5.7 (2.0)	9.4 (4.3)
HL	0.9	7.4 (2.2)	3.2 (1.1)	3.9 (1.8)
HLPH	1.2	9.3 (2.6)	3.4 (1.1)	3.9 (1.8)
LLPH	1.2	2.5 (0.7)	1.4 (0.5)	0.9 (0.4)
PLHH	1.6	10.3 (2.6)	6.9 (2.0)	10.1 (3.5)
HPHL	1.6	14.3 (3.6)	6.2 (1.8)	10.1 (3.5)
HH	2.3	13.6 (2.9)	5.9 (1.4)	8.2 (2.3)
LLHH	2.4	14.0 (2.9)	6.5 (1.5)	9.1 (2.5)
HHPLL	2.6	14.2 (2.8)	5.7 (1.3)	9.2 (2.4)
HLHP	2.7	11.9 (2.3)	4.5 (1.0)	6.4 (1.6)
LPHH	2.7	11.4 (2.2)	6.2 (1.3)	7.6 (1.9)
HHPL	2.9	14.2 (2.7)	6.4 (1.3)	8.1 (1.9)
LHPH	2.9	15.0 (2.8)	6.3 (1.3)	9.8 (2.3)
LH	3.0	12.1 (2.2)	6.1 (1.2)	9.2 (2.1)
LLPHH	3.0	9.3 (1.7)	4.8 (1.0)	3.1 (0.7)
HLH	3.2	14.0 (2.5)	4.3 (0.8)	6.5 (1.4)
LLPHHH	3.3	12.4 (2.2)	5.8 (1.1)	5.1 (1.1)
LHH	3.8	14.0 (2.3)	6.3 (1.1)	8.9 (1.7)
PHH	5.8	16.4 (2.0)	6.6 (0.9)	9.4 (1.3)
^a Antioxidative activity was evaluated by the ferric thiocyanate method. The assay was performed with 40 μM peptides, 100 μM BHA and BHT, and 10 μM tocopherol. The number in parentheses is the magnitude of synergistic effect: (activity of peptide + antioxidant) / (activity of peptide) + (activity of antioxidant). Data represent the mean of three replications.

Specific target protein(s)

N.D

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)N[C@@]([H])(CC1=CN=C-N1)C(=O)N1[C@@]([H])(CCC1)C(=O)O

Preparation method

Mode of preparation	Chemical synthesis
Enzyme(s)/starter culture	Peptides were prepared by the fluorenylmethoxycarbonyl (Fmoc)-strategy using a simultaneous multiple peptide synthesizer (model PSSM-8, Shimadzu).

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

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Matoba N, Yamada Y, Yoshikawa M. Design of a genetically modified soybean protein preventing hypertension based on an anti-hypertensive peptide derived from ovalbumin. Curr Med Chem Cardiovasc Hematol Agents. 2003 Jun;1(2):197-202. PMID: 15320699 DOI: 10.2174/1568016033477496
Other literature(s)	[1] Tsuge N, Eikawa Y, Nomura Y, et al. Antioxidative Activity of Peptides Prepared by Enzymatic Hydrolysis of Egg-white Albumin.[J]. Nippon Nogeikagaku Kaishi, 1991, 65(11):1635-1641. [2] Chen, H.M., et al., Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein. Journal of Agricultural and Food Chemistry, 1998. 46(1): p. 49-53. [3] Chen H M, Muramoto K, Yamauchi F. Structural Analysis of Antioxidative Peptides from Soybean. beta.-Conglycinin[J]. J.agric.food Chem, 1995, 43(3):574-578.
PubDate	2003