General Information

General Information

DRAVP ID DRAVPe01879

Peptide Name Pep19-4

Sequence GKKYRRFRWKFKFGKWFWFG

Sequence Length 20

UniProt ID No entry found

Source Synthetic construct

Activity Information

Target Organism HIV, HSV-1, HCV

Assay luciferase infection assay

Activity

[Ref.22457281]HIV-1 BaL:inhibition of viral entry in 293T cells(IC50=22 µg/ml);
HIV-1 NL4-3:inhibition of viral entry in 293T cells(IC50=10 µg/ml);
HSV-1:inhibition of viral entry in Vero cells(IC50=1.8 µg/ml);
Hepatitis C virus (HCV):inhibition of viral entry in 293T cells(IC50=37 µg/ml).

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

Cytotoxicity

[Ref.22457281]No significant cytotoxicity to Vero, TZM-bl and Jurkat cells even at a high concentration of 20 μg/mL.

Binding Target membrane

Mechanism SALPs block entry of a variety of human pathogenic enveloped viruses, such as HIV-1, HBV, HCV, and HSV 1 and 2 by blocking heparan sulfate on the host cell plasma membrane, which serves as a the docking molecule for these pathogens.

Structure Information

PDB ID None

Predicted Structure Download No predicted structure available

Linear/Cyclic Linear

N-terminal Modification Free

C-terminal Modification Free

Other Modification None

Stereochemistry L

Physicochemical Information

Formula C141H191N37O22

Absent amino acids ACDEHILMNPQSTV

Common amino acids FK

Mass 2756.3

Pl 11.76

Basic residues 8

Acidic residues 0

Hydrophobic residues 8

Net charge 8

Boman Index -4794

Hydrophobicity -121

Aliphatic Index 0

Half Life

Mammalian:30 hour
Yeast:>20 hour
E.coli:>10 hour

Extinction Coefficient cystines 17990

Absorbance 280nm 946.84

Polar residues 4

Literature Information

Literature 1

Title A new class of synthetic peptide inhibitors blocks attachment and entry of human pathogenic viruses.

Pubmed ID 22457281

Reference J Infect Dis. 2012 Jun;205(11):1654-64.

Author Krepstakies M, Lucifora J, Nagel CH, Zeisel MB, Holstermann B, Hohenberg H, Kowalski I, Gutsmann T, Baumert TF, Brandenburg K, Hauber J, Protzer U.

DOI 10.1093/infdis/jis273