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General Information
DRAVP ID DRAVPe02213
Peptide Name E30pep-wt
Sequence QLESLTDRELLLLIARKTCGSVE
Sequence Length 23
UniProt ID Q05323
Taxon ID 128952
Source Synthetic construct
Validation Experimentally Validated
Origin Information
Gene Name/ID VP30(911826)
GenBank Not Available
Amino Acid position 91-113
Domain Accession ID Not Available
Nucleotide sequence ID AF086833.2
Molecular Type Genomic RNA
Chromosomal Position Chromosome:8,509 - 9,375
Activity Information
Target Organism EBOV
Assay Virus inhibition assays
Activity
Hemolytic Activity No hemolysis information or data found in the reference(s) presented in this entry
Cytotoxicity No cytotoxicity information found in the reference(s) presented
Binding Target VP30
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
Linear/Cyclic Cyclic
N-terminal Modification Amination
C-terminal Modification Carboxylation
Other Modification None
Stereochemistry L
Physicochemical Information
Formula C111H195N31O37S1
Absent amino acids NHMFPWYOU
Common amino acids L
Mass 2588.01
Pl 4.87
Basic residues 3
Acidic residues 4
Hydrophobic residues 10
Net charge -1
Boman Index 1.71
Hydrophobicity 0.087
Aliphatic Index 135.67
Half Life
Extinction Coefficient cystines 0
Absorbance 280nm 0
Polar residues 5
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;278(43):41830-6.
Author Hartlieb B, Modrof J, Mühlberger E, et al.
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.