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 - DFBPAMIC0136(Antimicrobial peptide)

DFBP ID	DFBPAMIC0136
Peptide sequence	GFFALIPKIISSPLFKTLLSAVGSALSSSGGQE
Type	Native peptide
Peptide/Function name	Antimicrobial peptide, Pardaxin

Function-activity relationship

Main bioactivity	Antimicrobial activity
Otheir bioactivity	Anticancer 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

Peptide mass

Experimental mass	Theoretical mass
N.D	3323.81 Da ^c

Net charge

Isoelectric point (pI)

9.84 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.7455^c

Hydrophilic residue ratio

63.64%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Marine
Organism/Source	Red Sea moses sole, Pardachirus marmoratus
Precursor protein	Red Sea moses sole
Residue position	N.D
Precursor protein(s) search	No matching precursor protein found
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

Antimicrobial activity	Shai et al. demonstrated antibacterial activity in 1996. Active against E. coli, A. calcoaceticus, P. aeruginosa (25 uM), S. typhirnuriunz (40 uM), B. rnegateriurn, M. luteus, and B. subtilis (The MIC against other bacteria 3-13 uM). C-terminal amidation increased peptide activity.
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.

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

DFBP

[D1]	DFBPANCA0061
[D2]	DFBPMUFU0702

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Shai Y, Fox J, Caratsch C, Shih YL, Edwards C, Lazarovici P. Sequencing and synthesis of pardaxin, a polypeptide from the Red Sea Moses sole with ionophore activity. FEBS Lett. 1988 Dec 19;242(1):161-6. PMID: 2462511 DOI: 10.1016/0014-5793(88)81007-x
Other literature(s)	N.D
PubDate	1988