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 - DFBPAMIC0110(Antimicrobial peptide)

DFBP ID	DFBPAMIC0110
Peptide sequence	FFHHIFRGIVHVGKTIHRLVTG
Type	Native peptide
Peptide/Function name	Antimicrobial peptide, Piscidin 1

Function-activity relationship

Main bioactivity	Antimicrobial activity
Otheir bioactivity	Anticancer activity ^[D1]

Calculated physicochemical properties

Three-letter amino acid

Phe-Phe-His-His-Ile-Phe-Arg-Gly-Ile-Val-His-Val-Gly-Lys-Thr-Ile-His-Arg-Leu-Val-Thr-Gly

Single-letter amino acid

FFHHIFRGIVHVGKTIHRLVTG

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	2572.06 Da ^c

Net charge

Isoelectric point (pI)

12.52 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.4545^c

Hydrophilic residue ratio

59.09%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Hybrid striped bass (Morone saxatilis x Morone chrysops)
Precursor protein	Mast cells, gill, skin, intestine, spleen and anterior kidney
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

(1) anti-Gram+ & Gram-, antiviral, antifungal, anti-HIV, Mammalian cells, Cancer cells;
(2) First AMP isolated from mast cells. Active against E. coli, P. aeruginosa, S. typhimurium, B. subtilis, and S. aureus (MIC 1-4 uM) ^[1], including MRSA USA300 (MIC 3.1 uM) ^[2]. It is also active against channel catfish virus (CCV), frog virus 3 (FV3) ^[3] as well as HIV-1 (EC₅₀ = 1.4 uM) ^[4].

Table 1 Antibacterial activity of piscidins.
Bacteria	Minimum inhibitory concentration		Minimum bactericidal concentration
Bacteria	Piscidin 1	Piscidin 3	Piscidin 1	Piscidin 3
Fish pathogens
Streptococcus iniae (+)	3.1	3.1	3.1	3.1
Lactococcus garviae* (+)	3.1	6.3	3.1	12.5
L.garviaet (+)	3.1	3.1	3.1	6.3
Aeromonas salmonicida (-)	3.1	12.5	3.1	25.0
Aeromonas hydrophila (-)	0.8	1.6	0.8	1.6
Vibrio aiginolyticus (-)	3.1	6.3	3.1	6.3
Human pathogens
Staphylococcus aureus (+)	3.1	3.1	3.1	3.1
Streptococcus faecalis (+)	3.1	12.5	3.1	12.5
Escherichia coli (-)	3.1	3.1	3.1	3.1
Klebsiella pneumoniae (-)	3.1	6.3	3.1	6.3
Shigella flexneri (-)	3.1	6.3	3.1	6.3
Pseudomonas aeruginosa (-)	12.5	25.0	12.5	25.0

Specific target protein(s)

N.D

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	No prediction can be made about the peptide bitterness. ^prediction

SMILES

N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)NCC(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(C(C)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])([C@]([H])(O)C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)NCC(=O)O

Preparation method

Mode of preparation	Extract without enzyme
Enzyme(s)/starter culture	No enzyme

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]	DFBPANCA0385

[D2]

[D3]

[D4]

[D5]

Reference(s)

Primary literature	Silphaduang U, Noga EJ. Peptide antibiotics in mast cells of fish. Nature. 2001 Nov 15;414(6861):268-9. PMID: 11713517 DOI: 10.1038/35104690
Other literature(s)	[1] Structural flexibility and the positive charges are the key factors in bacterial cell selectivity and membrane penetration of peptoid-substituted analog of Piscidin 1. [2] Menousek J, Mishra B, Hanke M L, et al. Database screening and in vivo efficacy of antimicrobial peptides against meticillin-resistant Staphylococcus aureus USA300[J]. International Journal of Antimicrobial Agents, 2012, 39(5):402-6. [3] Chinchar V G, Bryan L, Silphadaung U, et al. Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides[J]. Virology, 2004, 323(2):268-75. [4] Wang G, Watson K M, Peterkofsky A, et al. Identification of Novel Human Immunodeficiency Virus Type 1-Inhibitory Peptides Based on the Antimicrobial Peptide Database[J]. Antimicrobial Agents & Chemotherapy, 2010, 54(3):1343-6.
PubDate	2001