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 - DFBPANPE0002(Antiviral peptide)

DFBP ID	DFBPANPE0002
Peptide sequence	LEYSI
Type	Native peptide
Peptide/Function name	Antiviral peptide

Function-activity relationship

Main bioactivity	Antiviral activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Leu-Glu-Tyr-Ser-Ile

Single-letter amino acid

LEYSI

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	623.69 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.34 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.5400^c

Hydrophilic residue ratio

40%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal, Marine
Organism/Source	Oyster
Precursor protein	Oyster proteins
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR1622 ---- Plant proteins ---- ATP synthase subunit alpha, mitochondrial Source.2: DFBPPR5064 ---- Plant proteins ---- ATP synthase subunit alpha, mitochondrial Source.3: DFBPPR6398 ---- Plant proteins ---- ATP synthase subunit alpha, mitochondrial Source.4: DFBPPR6809 ---- Plant proteins ---- ATP synthase subunit alpha, mitochondrial Source.5: DFBPPR7470 ---- Plant proteins ---- ATP synthase subunit alpha, mitochondrial Source.6: DFBPPR10206 ---- Animal proteins ---- Unconventional myosin-VI Source.7: DFBPPR10539 ---- Animal proteins ---- Netrin receptor UNC5C Source.8: DFBPPR15398 ---- Microorganism protein ---- Transcription activator of gluconeogenesis ERT1 Source.9: DFBPPR15468 ---- Microorganism protein ---- Mitochondrial inner membrane magnesium transporter LPE10 Source.10: DFBPPR8093 ---- Plant protein ---- ATP synthase subunit alpha, mitochondrial
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

Antiviral activity	Chemically synthesized Leu-Glu-Tyr-Ser-Ile showed HIV-1 protease (EC 3.4.23.16) inhibitory activity with an IC₅₀ value of 550 nM.
Specific target protein(s)	N.D

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Bitter taste ^prediction

SMILES

N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	The peptides inhibiting HIV-1 protease were isolated from the hydrolysate of oyster (Crassostrea gigas) proteins prepared with thermolysin.

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

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Lee TG, Maruyama S. Isolation of HIV-1 protease-inhibiting peptides from thermolysin hydrolysate of oyster proteins. Biochem Biophys Res Commun. 1998 Dec 30;253(3):604-8. PMID: 9918775 DOI: 10.1006/bbrc.1998.9824
Other literature(s)	N.D
PubDate	1998