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Studies of membranotropic and fusogenic activity of two putative HCV fusion peptides
- Source :
- Biochimica et Biophysica Acta:Biomembranes, Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2019, 1861 (1), pp.50-61. ⟨10.1016/j.bbamem.2018.10.011⟩
- Publication Year :
- 2019
-
Abstract
- International audience; Over the past decades, membranotropic peptides such as positively charged cell-penetrating peptides (CPPs) or amphipathic antimicrobial peptides (AMPs) have received increasing interest in order to improve therapeutic agent cellular uptake.As far as we are concerned, we were interested in studying HCV fusion peptides as putative anchors. Two peptides, HCV6 and HCV7, were identified and conjugated to a fluorescent tag NBD and tested for their interaction with liposomes as model membranes. DSC and spectrofluorescence analyses demonstrate HCV7 propensity to insert or internalize in vesicles containing anionic lipids DMPG whereas no activity was observed with zwitterionic DMPC. This behavior could be explained by the peptide sequence containing a cationic arginine residue. On the contrary, HCV6 did not exhibit any membranotropic activity but was the only sequence able to induce liposomes' fusion or aggregation monitored by spectrofluorescence and DLS. This two peptides mild activity was related to their inefficient structuration in contact with membrane mimetics, which was demonstrated by CD and NMR experiments.Altogether, our data allowed us to identify two promising membrane-active peptides from E1 and E2 HCV viral proteins, one fusogenic (HCV6) and the other membranotropic (HCV7). The latter was also confirmed by fluorescence microscopy with CHO cells, indicating that HCV7 could cross the plasma membrane via an endocytosis process. Therefore, this study provides new evidences supporting the identification of HCV6 as the HCV fusion peptide as well as insights on a novel membranotropic peptide from the HCV-E2 viral protein.
- Subjects :
- 0301 basic medicine
Magnetic Resonance Spectroscopy
Light
Lipid Bilayers
Peptide
Cell-Penetrating Peptides
Hepacivirus
medicine.disease_cause
Biochemistry
Mutagenesi
Protein Structure, Secondary
Viral Envelope Proteins
Cricetinae
Fluorescence Resonance Energy Transfer
Scattering, Radiation
HCV fusion peptide
Peptide sequence
chemistry.chemical_classification
Liposome
Microscopy
Spectrofluorescence
Antimicrobial Cationic Peptide
Calorimetry, Differential Scanning
Vesicle
Circular Dichroism
Membranotropic propertie
Hepatitis C
3. Good health
Fusogenic properties
Cricetulu
Fluorescent tag
Human
Viral protein
Recombinant Fusion Proteins
Antimicrobial peptides
Biophysics
HCV fusion peptides
CHO Cells
Endocytosis
Cell-Penetrating Peptide
03 medical and health sciences
Cricetulus
medicine
Animals
Humans
[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology
Fusogenic propertie
Hepaciviru
030102 biochemistry & molecular biology
Animal
Cell Membrane
Cell Biology
030104 developmental biology
chemistry
CHO Cell
Mutagenesis
Liposomes
Lipid Bilayer
Membranotropic properties
Antimicrobial Cationic Peptides
Recombinant Fusion Protein
Subjects
Details
- Language :
- English
- ISSN :
- 00052736 and 18792642
- Database :
- OpenAIRE
- Journal :
- Biochimica et Biophysica Acta:Biomembranes, Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2019, 1861 (1), pp.50-61. ⟨10.1016/j.bbamem.2018.10.011⟩
- Accession number :
- edsair.doi.dedup.....574535c6e767feb0e3ad5623f682cde6