Peptide Database

Peptide NameJEV(1959-1975)

Function Ontology

Antimicrobial

Antiviral

Antiviral ▸ Anti-Flavivirus ▸ Anti-Japanese encephalitis virus

Antiviral ▸ Anti-Flavivirus ▸ Anti-West Nile virus

Antiviral ▸ Anti-Hepatitis virus ▸ Anti-HCV

Antiviral ▸ Antiviral mechanism ▸ Viral replication inhibition ▸ Replication inhibitor

Enzyme modulation ▸ Enzyme inhibition ▸ Helicase inhibition

Standard StatusStandard

Sequence Length17 amino acids

Chemical FormulaC73H127N33O24

DescriptionStandard

        AAQRRGRVGRNPNQVGD
    

Molecular Weight1851.00 Da

Isoelectric Point (pI)12.00

Net Charge (pH 7.0)2.80

Net Charge (pH 7.4) 2.61

Charge Density (pH 7.0) 0.1647

GRAVY Index-1.55

Hydrophobic Moment 0.74

Boman Index-0.55

Instability Index24.82

Aliphatic Index 45.88

Aromaticity 0.0000

Extinction Coeff. Reduced 0.00

Extinction Coeff. Oxidized 0.00

The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.

Amino Acid Composition

TPSA 977.39

LogP -15.28

H-bond Donors 34.0

H-bond Acceptors 27.0

Rotatable Bonds 62.0

Heavy Atoms 130.0

Ring Count 1.0

Amide Bonds 20.0

3D PDB MODEL

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2D CHEMICAL STRUCTURE

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RECORD: Rec_0400515 VERIFIED: YES

Provenance & Taxonomy

Organismsynthetic construct [Synthetic]

FamilyProtein-derived synthetic peptide

Tax ID32630

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

N-TermNone

C-TermNone

Bio-Activity Profile

Function

Antiviral Anti-HCV Helicase inhibition

TargetHepatitis C virus (HCV)

Activity442±17.7 μM

MethodIC50

Half-LifeMammalian: 4.4 h; Yeast: >20 h; E. coli: >10 h

PaperViral NS3 helicase activity is inhibited by peptides reproducing the Arg-rich conserved motif of the enzyme (motif VI). | Borowski P, Heising MV, Miranda IB, Liao CL, Choe J, Baier A. | Biochem Pharmacol. 2008 Jul 1;76(1):28-38. | DOI:10.1016/j.bcp.2008.03.018 | PMID:18479669 PMID18479669 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/18479669/

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