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 - DFBPANOX0508(Antioxidative peptide)

DFBP ID	DFBPANOX0508
Peptide sequence	LANAK
Type	Native peptide
Peptide/Function name	Antioxidative peptide, SCAP1

Function-activity relationship

Main bioactivity	Antioxidative activity
Otheir bioactivity	Anticancer activity ^[D1], Multifunctional activity ^[D2]

Calculated physicochemical properties

Three-letter amino acid

Leu-Ala-Asn-Ala-Lys

Single-letter amino acid

LANAK

Peptide length

Peptide mass

Experimental mass	Theoretical mass
515.29 Da	515.60 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

10.04 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.0000^c

Hydrophilic residue ratio

60%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Oyster (Saccostrea cucullata)
Precursor protein	Oyster protein hydrolysates
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR5685 ---- Plant proteins ---- Protein ABERRANT POLLEN TRANSMISSION 1 Source.2: DFBPPR17648 ---- Animal proteins ---- NAD-capped RNA hydrolase NUDT12 Source.3: DFBPPR17917 ---- Animal proteins ---- Poly(ADP-ribose) glycohydrolase Source.4: DFBPPR20164 ---- Animal proteins ---- Glucosamine-6-phosphate isomerase 2 Source.5: DFBPPR12275 ---- Animal proteins ---- Ryanodine receptor 3 Source.6: DFBPPR15409 ---- Microorganism protein ---- Mitochondrial inner membrane magnesium transporter MRS2
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 LANAK showed potent DPPH-radical-scavenging activity (83.79 ± 0.53%) .
Specific target protein(s)	N.D

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Non-bitter taste ^prediction

SMILES

N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CC(=O)N)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CCCCN)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Oyster (S.cucullata) protein hydrolysate was recovered using enzymatic hydrolysis with protease from Bacillus cereus SU12.

Stability & Cytotoxicity

Peptide stability

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

Peptide cytotoxicity

Literature report:	No cytotoxic effect on human normal Vero cell lines by SCAP1 was observed. The results of the present study also confirm the ability of SCAP1 to protect normal cells. No cytotoxicity in normal cells compared to cancer cells is a prerequisite for any chemo-preventive agent.
Prediction:	ToxinPred

Additional information

The anticancer and antioxidative peptide (SCAP1) from oyster (S. cucullata) may be useful ingredients in pharmaceutical and nutraceutical applications.

Database cross-references

DFBP

[D1]	DFBPANCA0022
[D2]	DFBPMUFU0659

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Umayaparvathi, S., Meenakshi, S., Vimalraj, V., Arumugam, M., Sivagami, G., Balasubramanian, T. Antioxidant activity and anticancer effect of bioactive peptide from enzymatic hydrolysate of oyster (Saccostrea cucullata). Biomedicine & Preventive Nutrition. 2014, 4, 343-53. DOI: 10.1016/j.bionut.2014.04.006
Other literature(s)	[1] Zou, T.B., et al., The Structure-Activity Relationship of the Antioxidant Peptides from Natural Proteins. Molecules, 2016. 21(1): p. 72.
PubDate	2014