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General Information
DRAVP ID DRAVPe02309
Peptide Name 2-Chol
Sequence IEPHDWTKNITDKIDQIIHDFVDKGSGKKKKC
Sequence Length 32
UniProt ID No entry found
Taxon ID None
Source Synthetic construct
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 2-Chol was evaluated for its effectiveness against Ebola virus. The assay involved assessing the capacity of 2-Chol to inhibit GP-mediated viral entry using a vesicular stomatitis virus particle bearing the Ebola virus GP (VSV-GP) in place of the native glycoprotein G. The primary infection events were quantified by fluorescence confocal microscopy. Results showed that 2-Chol resulted in potent inhibition of VSV-GP entry, with approximately a 10^3-fold reduction in infection at 40 microM peptide concentrations. This level of inhibition was significantly higher than previously reported VSV-GP inhibition by Tat-Ebo at higher peptide concentrations. Notably, 2-Chol also exhibited potent activity for inhibiting VSV bearing its native envelope glycoprotein G (VSV-G), with over 90% reduction at 10 microM peptide concentration and more than 99% reduction at higher concentrations. Importantly, 2-Chol showed only modest cell toxicity under these conditions . Therefore, 2-Chol demonstrated potent inhibition of Ebola virus glycoprotein-mediated cell entry, suggesting a non-specific mechanism of neutralization that may involve a combination of peptide and cholesterol moieties.
Structure Information
PDB ID None
Linear/Cyclic Linear
N-terminal Modification cholesterylation
C-terminal Modification Free
Other Modification In the peptide sequence, the cysteine residue at position 32 is modified with a cholesterol (Chol) moiety. HIV-1 C-peptide conjugated to cholesterol contain covalent side chain-side chain crosslinks to promote an alpha-helical conformation. The cholesterol-conjugated C-peptides proved to be potent inhibitors of Ebola virus glycoprotein (GP)-mediated cell entry (~10^3-fold reduction in infection at 40 microM
Stereochemistry L
Physicochemical Information
Formula C166H266N46O50S1
Absent amino acids ALMORUY
Common amino acids K
Mass 3738.28
Pl 8.12
Basic residues 7
Acidic residues 6
Hydrophobic residues 8
Net charge 1
Boman Index 2.56
Hydrophobicity -1.1
Aliphatic Index 70
Half Life
Extinction Coefficient cystines 5500
Absorbance 280nm 1.471
Polar residues 21
Literature Information
Literature 1
Title C-peptide inhibitors of Ebola virus glycoprotein-mediated cell entry: effects of conjugation to cholesterol and side chain-side chain crosslinking
Pubmed ID 23962564
Reference Bioorg Med Chem Lett. 2013;23(19):5356-60.
Author Higgins CD, Koellhoffer JF, Chandran K
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.