To the extent possible under law, the person who associated CC0 with this work has waived all copyright and related or neighboring rights to this work.
General Information
DRAVP ID DRAVPe02014
Peptide Name E30pep-wt
Sequence QLESLTDRELLLLIARKTCGSVE
Sequence Length 23
UniProt ID Q05323
Source Synthetic construct
Activity Information
Target Organism EBOV
Assay Immunofluorescence
Activity
Hemolytic Activity No hemolysis information or data found in the reference(s) presented in this entry
Cytotoxicity
Binding Target Transcription
Mechanism E30pep-wt seemed to bind efficiently to VP30 and consequently blocked the oligomerization of the protein. When E30pep-wt was transfected into EBOV-infected cells, the peptide inhibited viral replication suggesting that inhibition of VP30 oligomerization represents a target for EBOV antiviral drugs.
Structure Information
PDB ID None
Predicted Structure Download No predicted structure available
Linear/Cyclic Linear
N-terminal Modification Free
C-terminal Modification Amidation
Other Modification None
Stereochemistry L
Physicochemical Information
Formula C111H195N31O37S
Absent amino acids FHMNPWY
Common amino acids L
Mass 2588.01
Pl 4.87
Basic residues 3
Acidic residues 4
Hydrophobic residues 9
Net charge -1
Boman Index -3951
Hydrophobicity 8.7
Aliphatic Index 135.65
Half Life
Extinction Coefficient cystines 0
Absorbance 280nm 0
Polar residues 6
Literature Information
Literature 1
Title Oligomerization of Ebola virus VP30 is essential for viral transcription and can be inhibited by a synthetic peptide.
Pubmed ID 12912982
Reference J Biol Chem. 2003 Oct 24;278(43):41830-6.
Author Hartlieb B, Modrof J, Mühlberger E, Klenk HD, Becker S.
To the extent possible under law, the person who associated CC0 with this work has waived all copyright and related or neighboring rights to this work.