General Information
DRAVP ID DRAVPe02314
Peptide Name EBOV-3
Sequence IEPHDWTKNITDKIDQIIHDFVDKTLPDQG
Sequence Length 30
UniProt ID No entry found
Taxon ID None
Source Cholesterol-conjugated synthetic peptide
Validation Experimentally Validated
Origin Information
Gene Name/ID Not Available
GenBank Not Available
Amino Acid position Not Available
Domain Accession ID Not Available
Nucleotide sequence ID Not Available
Molecular Type Not Available
Chromosomal Position Not Available
Activity Information
Target Organism EBOV
Assay Not Available
Activity
Hemolytic Activity No hemolysis information or data found in the reference(s) presented in this entry
Cytotoxicity
Binding Target Glycoprotein.
Mechanism EBOV-3 is an elongated peptide with five residues downstream of the helical domain. This modification likely contributes to the peptide's potency in inhibiting EBOV infection. By targeting specific regions of the EBOV glycoprotein, EBOV-3 interferes with viral entry and replication processes, ultimately inhibiting the virus's ability to infect host cells
Structure Information
PDB ID None
Linear/Cyclic Cyclic
N-terminal Modification cholesterylation
C-terminal Modification PEG4
Other Modification In the peptide sequence, the cysteine residue at position 31 is modified with a PEG4-cholesterol (PEG4-Chol) moiety.
Stereochemistry L
Physicochemical Information
Formula C158H243N41O51
Absent amino acids ACMORSUY
Common amino acids D
Mass 3532.91
Pl 4.52
Basic residues 3
Acidic residues 7
Hydrophobic residues 9
Net charge -4
Boman Index 2.35
Hydrophobicity -0.88
Aliphatic Index 87.67
Half Life
Extinction Coefficient cystines 5500
Absorbance 280nm 1.557
Polar residues 18
Literature Information
Literature 1
Title Cholesterol-conjugated stapled peptides inhibit Ebola and Marburg viruses in vitro and in vivo
Pubmed ID 31473342
Reference Antiviral Res. 2019;171:104592.
Author Pessi A, Bixler SL, Soloveva V, et al