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 - DFBPANPE0001(Antiviral peptide)

DFBP ID	DFBPANPE0001
Peptide sequence	LLEYSI
Type	Native peptide
Peptide/Function name	Antiviral peptide, Protease HIV1 inhibitor

Function-activity relationship

Main bioactivity	Antiviral activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Leu-Leu-Glu-Tyr-Ser-Ile

Single-letter amino acid

LLEYSI

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	736.84 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.34 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

1.0833^c

Hydrophilic residue ratio

50%^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	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

Antiviral activity	Chemically synthesized Leu-Leu-Glu-Tyr-Ser-Ile showed IC₅₀ value of 20 nM, and behaved as competitive inhibitor for HIV-1 protease (EC 3.4.23.16) with K_i values of 13 nM. The peptides were more potent as an HIV-1 protease inhibitor than pepstatin A.
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])(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