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List of peptide properties
DFBP ID - DFBPANCA0061(Anticancer peptide)
DFBP ID DFBPANCA0061
Peptide sequence GFFALIPKIISSPLFKTLLSAVGSALSSSGGQE
Type Native peptide
Peptide/Function name Anticancer peptide, Pardaxin
Function-activity relationship
Main bioactivity Anticancer activity
Otheir bioactivity Antimicrobial activity [D1], Multifunctional activity [D2]
Calculated physicochemical properties
Three-letter amino acid Gly-Phe-Phe-Ala-Leu-Ile-Pro-Lys-Ile-Ile-Ser-Ser-Pro-Leu-Phe-Lys-Thr-Leu-Leu-Ser-Ala-Val-Gly-Ser-Ala-Leu-Ser-Ser-Ser-Gly-Gly-Gln-Glu
Single-letter amino acid GFFALIPKIISSPLFKTLLSAVGSALSSSGGQE
Peptide length 33
Peptide mass
Experimental mass Theoretical mass
N.D 3323.81 Da c
Net charge 0.00 c
Isoelectric point (pI) 9.84 c
IC50 N.D
pIC50 N.D
GRAVY 0.7455 c
Hydrophilic residue ratio 63.64% c
Peptide calculator
To calculate the physicochemical properties of bioactive peptide.
Peptide source & Food-borne protein(s) search
Classification Animal, Marine, Fish
Organism/Source Pardachirus marmoratus
Precursor protein Red Sea moses sole [2]
Residue position N.D
Precursor protein(s) search
No matching precursor protein found
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

Pardaxin reduced cell viability in a dose-dependent manner. The expression of activated caspase-3 in SCC-4 cells significantly increased after 24-h treatment with pardaxin. Pardaxin treatment resulted in the cell cycle arrest of SCC-4 cells in the G2/M phase, thereby limiting cell proliferation. Furthermore, pardaxin treatment substantially alleviated carcinogenesis in the DMBA-induced hamster buccal pouch model by lowering prostaglandin E2 levels.

Tumor target
Mechanism
Solid tumor cells
Membrane permeabilization
Specific target protein(s) N.D
Taste properties & Structure
Bitterness
Literature report N.D
Bitter prediction tools Non-bitter taste prediction
SMILES NCC(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CO)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(C(C)C)C(=O)NCC(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CO)C(=O)NCC(=O)NCC(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)O
Preparation method
Mode of preparation

Synthesis

Enzyme(s)/starter culture

No enzyme, Pardaxin was synthesized by the solid-phase method [2].

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

Pardaxin is a potential marine drug for adjuvant chemotherapy for human OSCC and oral cancer.

Database cross-references
DFBP
[D1] DFBPAMIC0136
[D2] DFBPMUFU0702
BIOPEP-UWM [D3] -
APD [D4] -
BioPepDB [D5] -
MBPDB [D6] -
Reference(s)
Primary literature Han Y, Cui Z, Li YH, Hsu WH, Lee BH. In Vitro and in Vivo Anticancer Activity of Pardaxin against Proliferation and Growth of Oral Squamous Cell Carcinoma. Mar Drugs. 2015 Dec 23;14(1):2.
PMID: 26703631
Other literature(s)

[1] Deslouches B, Di Y P. Antimicrobial peptides with selective antitumor mechanisms: prospect for anticancer applications:[J]. Oncotarget, 2017, 8(28):46635-46651.
[2] Shai Y, Fox J, Caratsch C, et al. Sequencing and synthesis of pardaxin, a polypeptide from the Red Sea Moses sole with ionophore activity[J]. Febs Letters, 1988, 242(1):161-166.

PubDate 2015
Copyright © 2020. Record / license number: Chongqing ICP No. 2000214