Membrane anchorage brings about fusogenic properties in a short synthetic peptide
| Autor: | and Alain Bienvenüe, § Josette Sainte-Marie, Jean R. Philippot, Eve-Isabelle Pécheur, Luc Maurin, Dick Hoekstra |
|---|---|
| Přispěvatelé: | Nanotechnology and Biophysics in Medicine (NANOBIOMED), Deleage, Gilbert, Institut de biologie et chimie des protéines [Lyon] (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 1997 |
| Předmět: |
Population
Biotin LIPOSOMES PROTEIN Peptide Biology Biochemistry Membrane Fusion Fluorescence Glycerides VESICLES 03 medical and health sciences chemistry.chemical_compound [SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology HEMIFUSION [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology education 030304 developmental biology Fluorescent Dyes SENDAI VIRUS chemistry.chemical_classification Phosphatidylethanolamine 0303 health sciences education.field_of_study Liposome Vesicle Lysine Phosphatidylethanolamines 030302 biochemistry & molecular biology Lipid bilayer fusion SNAP25 Lysophosphatidylcholines Hydrogen-Ion Concentration N-TERMINAL PEPTIDES ENVELOPE GLYCOPROTEIN FUSION PEPTIDE INFLUENZA HEMAGGLUTININ Kinetics Membrane chemistry HUMAN-IMMUNODEFICIENCY-VIRUS Biophysics Oligopeptides |
| Zdroj: | Biochemistry, 36(13), 3773-3781. AMER CHEMICAL SOC Biochemistry Biochemistry, American Chemical Society, 1997, 36, pp.3773-3781 |
| ISSN: | 0006-2960 1520-4995 |
| Popis: | International audience; The fusogenic properties of an amphipathic net-negative peptide (wae 11), consisting of 11 amino acid residues, were studied. We demonstrate that, whereas the free peptide displays no significant fusion activity, membrane fusion is strongly promoted when the peptide is anchored to a liposomal membrane. The fusion activity of the peptide appears to be independent of pH, and membrane merging is an essentially nonleaky process. Thus, the extents of lipid mixing and contents mixing were virtually indistinguishable. Vesicle aggregation is a prerequisite for fusion. For this process to take place, the target membranes required a positive charge which was provided by incorporating lysine-coupled phosphatidylethanolamine (PElys). The coupled peptide, present in one population, could thus cause vesicle aggregation via nonspecific electrostatic interaction with PElys. However, the free peptide failed to induce aggregation of PElys vesicles, suggesting that the spatial orientation of the coupled peptide codetermined its ability to bring about vesicle aggregation and fusion. With the monitoring of changes in the intrinsic Trp fluorescence, in conjunction with KI-quenching studies, it would appear that hydrophobic interactions facilitate the fusion event, possibly involving (partial) peptide penetration. Such a penetration may be needed to trigger formation of a transient, nonbilayer structure. Since lysophosphatidylcholine inhibited while monoolein strongly stimulated peptide-induced fusion, our data indicate that wae 11-induced fusion proceeds according to a model consistent with the stalk-pore hypothesis for membrane fusion.The fusogenic properties of an amphipathic net-negative peptide (wae 11), consisting of 11 amino acid residues, were studied. We demonstrate that, whereas the free peptide displays no significant fusion activity, membrane fusion is strongly promoted when the peptide is anchored to a liposomal membrane. The fusion activity of the peptide appears to be independent of pH, and membrane merging is an essentially nonleaky process. Thus, the extents of lipid mixing and contents mixing were virtually indistinguishable. Vesicle aggregation is a prerequisite for fusion. For this process to take place, the target membranes required a positive charge which was provided by incorporating lysine-coupled phosphatidylethanolamine (PElys). The coupled peptide, present in one population, could thus cause vesicle aggregation via nonspecific electrostatic interaction with PElys. However, the free peptide failed to induce aggregation of PElys vesicles, suggesting that the spatial orientation of the coupled peptide codetermined its ability to bring about vesicle aggregation and fusion. With the monitoring of changes in the intrinsic Trp fluorescence, in conjunction with KI-quenching studies, it would appear that hydrophobic interactions facilitate the fusion event, possibly involving (partial) peptide penetration. Such a penetration may be needed to trigger formation of a transient, nonbilayer structure. Since lysophosphatidylcholine inhibited while monoolein strongly stimulated peptide-induced fusion, our data indicate that wae 11-induced fusion proceeds according to a model consistent with the stalk-pore hypothesis for membrane fusion. |
| Databáze: | OpenAIRE |
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