General Information


DRAVP ID  DRAVPe00118

Peptide Name   P34(derived from E2 envelope protein of GB virus C)

Sequence  SWFASTGGRDSKIDVWSL

Sequence Length  18

UniProt ID  No entry found

Source  Synthetic construct(derived from E2 envelope protein of GB virus C)



Activity Information


Target Organism  HIV

Assay  Gp41-Mediated Cell-Cell Fusion Assay

Activity 

  • [Ref.20718496]HIV-1:inhibition of HIV(HXB2) infection in TZM-bl Cells(IC50=237.4 μM);inhibition of HIV(BAL) infection in TZM-bl Cells(IC50=411.2 μM);inhibition of HIV(69-7) infection in TZM-bl Cells(IC50=118.6 μM).

Hemolytic Activity  No hemolysis information or data found in the reference(s) presented in this entry

Cytotoxicity 

  • No cytotoxicity information or data found in the reference(s) presented in this entry

Binding Target  membrane

Mechanism  E2 GBV-C domain interferes with the HIV-1 fusion peptide-vesicle interaction, produce a notable decrease the cellular membrane fusion, and interfere with the HIV-1 infectivity in a dose-dependent manner.



Structure Information


PDB ID  None

Predicted Structure Download  DRAVPe00118

Linear/Cyclic  Linear

N-terminal Modification  Free

C-terminal Modification  Free

Other Modification  None

Stereochemistry  L



Physicochemical Information


Formula  C91H134N24O28

Absent amino acids  CEHMNPQY

Common amino acids  S

Mass  2012.21

Pl  5.68

Basic residues  2

Acidic residues  2

Hydrophobic residues  7

Net charge  0

Boman Index  -2887

Hydrophobicity  -26.67

Aliphatic Index  65

Half Life 

  •     Mammalian:1.9 hour
  •     Yeast:>20 hour
  •     E.coli:>10 hour

Extinction Coefficient cystines  11000

Absorbance 280nm  647.06

Polar residues  7



Literature Information


Literature 1

Title   Effect of synthetic peptides belonging to E2 envelope protein of GB virus C on human immunodeficiency virus type 1 infection.

Pubmed ID   20718496

Reference   J Med Chem. 2010 Aug 26;53(16):6054-63. 

Author   Herrera E, Tenckhoff S, Gómara MJ, Galatola R, Bleda MJ, Gil C, Ercilla G, Gatell JM, Tillmann HL, Haro I.

DOI   10.1021/jm100452c