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List of peptide properties
DFBP ID - DFBPANCA0022(Anticancer peptide)
DFBP ID DFBPANCA0022
Peptide sequence LANAK
Type Native peptide
Peptide/Function name Anticancer peptide, SCAP1
Function-activity relationship
Main bioactivity Anticancer activity
Otheir bioactivity Antioxidative activity [D1], Multifunctional activity [D2]
Calculated physicochemical properties
Three-letter amino acid Leu-Ala-Asn-Ala-Lys
Single-letter amino acid LANAK
Peptide length 5
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
To calculate the physicochemical properties of bioactive peptide.
Peptide source & Food-borne protein(s) search
Classification Animal, Marine
Organism/Source Oyster (Saccostrea cucullata)
Precursor protein Oyster (Saccostrea cucullata) protein hydrolysates
Residue position N.D
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
Anticancer activity

Induced cell growth inhibition, apoptotic changes and oxidative DNA damage:

  1. Oyster peptide SCAP1 showed a noticeable dose- and time-dependent anticancer activity against human colon carcinoma (HT-29) cell lines. SCAP1 displayed cytotoxic activity on colon cancer cells with IC50 values of 90.31 ± 0.45 μg/ml, 70.87 ± 0.82 μg/ml, and 60.21 ± 0.45 μg/ml for 24, 48 and 72 h of incubation respectively. In addition, no cytotoxic effect on human normal Vero cell lines by SCAP1 was observed.

  2. Dual-staining (AO-EBr) and Hoechst 33258 staining assays revealed that SCAP1 induced apoptosis in HT-29 cells. Peptide treatment significantly increased apoptotic morphological changes in HT-29 cells.

  3. Different grades of DNA damage were observed in peptide (SCAP1) treated cells at 24, 48 and 72 h of incubation. Among these, 72 h of peptide treatment showed fragmented DNA. The amount of DNA damage reaches about 3 folds to the control value after 72h of peptide (SCAP1) treatment.

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
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] DFBPANOX0508
[D2] DFBPMUFU0659
BIOPEP-UWM [D3] 8994
APD [D4] -
BioPepDB [D5] -
MBPDB [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.
Other literature(s)

[1] Chalamaiah M, Yu W, Wu J. Immunomodulatory and anticancer protein hydrolysates (peptides) from food proteins: A review.[J]. Food Chemistry, 2018, 245:205-222.

PubDate 2014
Copyright © 2020. Record / license number: Chongqing ICP No. 2000214