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 - DFBPHAPE0022(Haemolytic peptide)

DFBP ID	DFBPHAPE0022
Peptide sequence	GWGSFFKKAAHVGKHVGKAALTHYL
Type	Native peptide
Peptide/Function name	Haemolytic peptide, Pleurocidin (Ple)

Function-activity relationship

Main bioactivity	Haemolytic activity
Otheir bioactivity	Antimicrobial activity ^[D1], Anticancer activity ^[D2], Multifunctional activity ^[D3]

Calculated physicochemical properties

Three-letter amino acid

Gly-Trp-Gly-Ser-Phe-Phe-Lys-Lys-Ala-Ala-His-Val-Gly-Lys-His-Val-Gly-Lys-Ala-Ala-Leu-Thr-His-Tyr-Leu

Single-letter amino acid

GWGSFFKKAAHVGKHVGKAALTHYL

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	2711.16 Da ^c

Net charge

Isoelectric point (pI)

10.64 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.0680^c

Hydrophilic residue ratio

60%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal, Fish, Marine
Organism/Source	Winter flounder (Pleuronectes americanus)
Precursor protein	The skin-secreted mucous of the winter flounder.
Residue position	N.D
Precursor protein(s) search	No matching precursor protein found
Link-research Inductive analysis	Link 1: DFBPHAPE0023----Winter flounder----Pleurocidin

Biological/Functional activity & target protein

Haemolytic activity

The effective bioactive sequence of the peptide was GWGSFFKKAAHVGKHVGKAALTHYL-NH₂ and showed broad spectrum of antimicrobial and hemolytic activity.

Table 1 Antifungal activity of Ple and Melittin
Peptides	MIC (uM)
Peptides	S. cerevisiae	T. beigelii	C. albicans
Pleurocidin	5	2.5	5
Melittin	1.25	0.63	1.25

Table 2 Hemolytic activity of Ple and Melittin against human erythrocyte cells
Peptides	% Hemolysis (uM)
Peptides	100	50	25	12.5	6.25	3.12
Pleurocidin	77	29	6	0	0	0
Melittin	100	100	100	100	100	98

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])(CC(=CN2)C1=C2C=CC=C1)C(=O)NCC(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])(C(C)C)C(=O)NCC(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])(C(C)C)C(=O)NCC(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CC(C)C)C(=O)O

Preparation method

Mode of preparation	Chemical synthesis
Enzyme(s)/starter culture	The peptides were synthesized by the solid-phase method using Fmoc (9-fluorenyl-methoxycarbonyl)-chemistry.

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

(1) The antifungal activities of the peptides were comparable to that of melittin (GIGAVLKVLTTGLPALISWIKRKRQQ-NH₂), the most widely known amphipathic, and membrane-lytic α-helical peptide, which has also been known to possess broad antimicrobial activity due to the formation of membrane pores and it has strong hemolytic activity toward mamalian cells.
(2) The α-Helicity of Pleurocidin is 60%.

Database cross-references

DFBP

[D1]	DFBPAMIC0033, DFBPAMIC0171
[D2]	DFBPANCA0657, DFBPANCA0658
[D3]	DFBPMUFU0699

[D4]

[D5]

[D6]

[D7]

Reference(s)

Primary literature	Sung WS, Lee DG. Pleurocidin-derived antifungal peptides with selective membrane-disruption effect. Biochem Biophys Res Commun. 2008 May 9;369(3):858-61. PMID: 18325325 DOI: 10.1016/j.bbrc.2008.02.109
Other literature(s)	[1] Cole A M, Weis P, Diamond G. Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder.[J]. Journal of Biological Chemistry, 1997, 272(18):12008-12013.
PubDate	2008