Dengue fusion peptide in Langmuir monolayers: A binding parameter study
Membrane fusion is known to be the primary mechanism of entry of flaviviruses into host cells. Several studies reported the investigation of the membrane fusion mechanism mediated by the fusion peptide, a component of the membrane protein surrounding the flaviviruses. In this study, we investigated...
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Gespeichert in:
| Autor*in: |
Schmidt, Thaís F. [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2021transfer abstract |
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| Übergeordnetes Werk: |
Enthalten in: “We can and should do better” - an interview with the 2020 Nobel prize laureates who revolutionized hepatology - Baumert, Thomas F. ELSEVIER, 2021, an international journal devoted to the physics and chemistry of biological phenomena, Amsterdam [u.a.] |
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| Übergeordnetes Werk: |
volume:271 ; year:2021 ; pages:0 |
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| DOI / URN: |
10.1016/j.bpc.2021.106553 |
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| 520 | |a Membrane fusion is known to be the primary mechanism of entry of flaviviruses into host cells. Several studies reported the investigation of the membrane fusion mechanism mediated by the fusion peptide, a component of the membrane protein surrounding the flaviviruses. In this study, we investigated the interaction of Dengue fusion peptide (FLAg) with Langmuir monolayers to uncover the role of membrane charges and organization in its membrane binding. Binding parameters of FLAg were obtained by measuring its adsorption onto Langmuir monolayers of different types of individual lipids, as well as their mixtures. Specific peptide binding was observed in the presence of charged lipid monolayers at different pHs, revealing that the lipid composition of the membrane modulates peptide interaction, and the preference of the peptide for negatively charged lipids. | ||
| 520 | |a Membrane fusion is known to be the primary mechanism of entry of flaviviruses into host cells. Several studies reported the investigation of the membrane fusion mechanism mediated by the fusion peptide, a component of the membrane protein surrounding the flaviviruses. In this study, we investigated the interaction of Dengue fusion peptide (FLAg) with Langmuir monolayers to uncover the role of membrane charges and organization in its membrane binding. Binding parameters of FLAg were obtained by measuring its adsorption onto Langmuir monolayers of different types of individual lipids, as well as their mixtures. Specific peptide binding was observed in the presence of charged lipid monolayers at different pHs, revealing that the lipid composition of the membrane modulates peptide interaction, and the preference of the peptide for negatively charged lipids. | ||
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10.1016/j.bpc.2021.106553 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001321.pica (DE-627)ELV053331885 (ELSEVIER)S0301-4622(21)00013-2 DE-627 ger DE-627 rakwb eng 610 VZ 44.87 bkl Schmidt, Thaís F. verfasserin aut Dengue fusion peptide in Langmuir monolayers: A binding parameter study 2021transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Membrane fusion is known to be the primary mechanism of entry of flaviviruses into host cells. Several studies reported the investigation of the membrane fusion mechanism mediated by the fusion peptide, a component of the membrane protein surrounding the flaviviruses. In this study, we investigated the interaction of Dengue fusion peptide (FLAg) with Langmuir monolayers to uncover the role of membrane charges and organization in its membrane binding. Binding parameters of FLAg were obtained by measuring its adsorption onto Langmuir monolayers of different types of individual lipids, as well as their mixtures. Specific peptide binding was observed in the presence of charged lipid monolayers at different pHs, revealing that the lipid composition of the membrane modulates peptide interaction, and the preference of the peptide for negatively charged lipids. Membrane fusion is known to be the primary mechanism of entry of flaviviruses into host cells. Several studies reported the investigation of the membrane fusion mechanism mediated by the fusion peptide, a component of the membrane protein surrounding the flaviviruses. In this study, we investigated the interaction of Dengue fusion peptide (FLAg) with Langmuir monolayers to uncover the role of membrane charges and organization in its membrane binding. Binding parameters of FLAg were obtained by measuring its adsorption onto Langmuir monolayers of different types of individual lipids, as well as their mixtures. Specific peptide binding was observed in the presence of charged lipid monolayers at different pHs, revealing that the lipid composition of the membrane modulates peptide interaction, and the preference of the peptide for negatively charged lipids. Riske, Karin A. oth Caseli, Luciano oth Salesse, Christian oth Enthalten in Elsevier Science Baumert, Thomas F. ELSEVIER “We can and should do better” - an interview with the 2020 Nobel prize laureates who revolutionized hepatology 2021 an international journal devoted to the physics and chemistry of biological phenomena Amsterdam [u.a.] (DE-627)ELV006315437 volume:271 year:2021 pages:0 https://doi.org/10.1016/j.bpc.2021.106553 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.87 Gastroenterologie VZ AR 271 2021 0 |
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10.1016/j.bpc.2021.106553 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001321.pica (DE-627)ELV053331885 (ELSEVIER)S0301-4622(21)00013-2 DE-627 ger DE-627 rakwb eng 610 VZ 44.87 bkl Schmidt, Thaís F. verfasserin aut Dengue fusion peptide in Langmuir monolayers: A binding parameter study 2021transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Membrane fusion is known to be the primary mechanism of entry of flaviviruses into host cells. Several studies reported the investigation of the membrane fusion mechanism mediated by the fusion peptide, a component of the membrane protein surrounding the flaviviruses. In this study, we investigated the interaction of Dengue fusion peptide (FLAg) with Langmuir monolayers to uncover the role of membrane charges and organization in its membrane binding. Binding parameters of FLAg were obtained by measuring its adsorption onto Langmuir monolayers of different types of individual lipids, as well as their mixtures. Specific peptide binding was observed in the presence of charged lipid monolayers at different pHs, revealing that the lipid composition of the membrane modulates peptide interaction, and the preference of the peptide for negatively charged lipids. Membrane fusion is known to be the primary mechanism of entry of flaviviruses into host cells. Several studies reported the investigation of the membrane fusion mechanism mediated by the fusion peptide, a component of the membrane protein surrounding the flaviviruses. In this study, we investigated the interaction of Dengue fusion peptide (FLAg) with Langmuir monolayers to uncover the role of membrane charges and organization in its membrane binding. Binding parameters of FLAg were obtained by measuring its adsorption onto Langmuir monolayers of different types of individual lipids, as well as their mixtures. Specific peptide binding was observed in the presence of charged lipid monolayers at different pHs, revealing that the lipid composition of the membrane modulates peptide interaction, and the preference of the peptide for negatively charged lipids. Riske, Karin A. oth Caseli, Luciano oth Salesse, Christian oth Enthalten in Elsevier Science Baumert, Thomas F. ELSEVIER “We can and should do better” - an interview with the 2020 Nobel prize laureates who revolutionized hepatology 2021 an international journal devoted to the physics and chemistry of biological phenomena Amsterdam [u.a.] (DE-627)ELV006315437 volume:271 year:2021 pages:0 https://doi.org/10.1016/j.bpc.2021.106553 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.87 Gastroenterologie VZ AR 271 2021 0 |
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10.1016/j.bpc.2021.106553 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001321.pica (DE-627)ELV053331885 (ELSEVIER)S0301-4622(21)00013-2 DE-627 ger DE-627 rakwb eng 610 VZ 44.87 bkl Schmidt, Thaís F. verfasserin aut Dengue fusion peptide in Langmuir monolayers: A binding parameter study 2021transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Membrane fusion is known to be the primary mechanism of entry of flaviviruses into host cells. Several studies reported the investigation of the membrane fusion mechanism mediated by the fusion peptide, a component of the membrane protein surrounding the flaviviruses. In this study, we investigated the interaction of Dengue fusion peptide (FLAg) with Langmuir monolayers to uncover the role of membrane charges and organization in its membrane binding. Binding parameters of FLAg were obtained by measuring its adsorption onto Langmuir monolayers of different types of individual lipids, as well as their mixtures. Specific peptide binding was observed in the presence of charged lipid monolayers at different pHs, revealing that the lipid composition of the membrane modulates peptide interaction, and the preference of the peptide for negatively charged lipids. Membrane fusion is known to be the primary mechanism of entry of flaviviruses into host cells. Several studies reported the investigation of the membrane fusion mechanism mediated by the fusion peptide, a component of the membrane protein surrounding the flaviviruses. In this study, we investigated the interaction of Dengue fusion peptide (FLAg) with Langmuir monolayers to uncover the role of membrane charges and organization in its membrane binding. Binding parameters of FLAg were obtained by measuring its adsorption onto Langmuir monolayers of different types of individual lipids, as well as their mixtures. Specific peptide binding was observed in the presence of charged lipid monolayers at different pHs, revealing that the lipid composition of the membrane modulates peptide interaction, and the preference of the peptide for negatively charged lipids. Riske, Karin A. oth Caseli, Luciano oth Salesse, Christian oth Enthalten in Elsevier Science Baumert, Thomas F. ELSEVIER “We can and should do better” - an interview with the 2020 Nobel prize laureates who revolutionized hepatology 2021 an international journal devoted to the physics and chemistry of biological phenomena Amsterdam [u.a.] (DE-627)ELV006315437 volume:271 year:2021 pages:0 https://doi.org/10.1016/j.bpc.2021.106553 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.87 Gastroenterologie VZ AR 271 2021 0 |
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10.1016/j.bpc.2021.106553 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001321.pica (DE-627)ELV053331885 (ELSEVIER)S0301-4622(21)00013-2 DE-627 ger DE-627 rakwb eng 610 VZ 44.87 bkl Schmidt, Thaís F. verfasserin aut Dengue fusion peptide in Langmuir monolayers: A binding parameter study 2021transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Membrane fusion is known to be the primary mechanism of entry of flaviviruses into host cells. Several studies reported the investigation of the membrane fusion mechanism mediated by the fusion peptide, a component of the membrane protein surrounding the flaviviruses. In this study, we investigated the interaction of Dengue fusion peptide (FLAg) with Langmuir monolayers to uncover the role of membrane charges and organization in its membrane binding. Binding parameters of FLAg were obtained by measuring its adsorption onto Langmuir monolayers of different types of individual lipids, as well as their mixtures. Specific peptide binding was observed in the presence of charged lipid monolayers at different pHs, revealing that the lipid composition of the membrane modulates peptide interaction, and the preference of the peptide for negatively charged lipids. Membrane fusion is known to be the primary mechanism of entry of flaviviruses into host cells. Several studies reported the investigation of the membrane fusion mechanism mediated by the fusion peptide, a component of the membrane protein surrounding the flaviviruses. In this study, we investigated the interaction of Dengue fusion peptide (FLAg) with Langmuir monolayers to uncover the role of membrane charges and organization in its membrane binding. Binding parameters of FLAg were obtained by measuring its adsorption onto Langmuir monolayers of different types of individual lipids, as well as their mixtures. Specific peptide binding was observed in the presence of charged lipid monolayers at different pHs, revealing that the lipid composition of the membrane modulates peptide interaction, and the preference of the peptide for negatively charged lipids. Riske, Karin A. oth Caseli, Luciano oth Salesse, Christian oth Enthalten in Elsevier Science Baumert, Thomas F. ELSEVIER “We can and should do better” - an interview with the 2020 Nobel prize laureates who revolutionized hepatology 2021 an international journal devoted to the physics and chemistry of biological phenomena Amsterdam [u.a.] (DE-627)ELV006315437 volume:271 year:2021 pages:0 https://doi.org/10.1016/j.bpc.2021.106553 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.87 Gastroenterologie VZ AR 271 2021 0 |
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10.1016/j.bpc.2021.106553 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001321.pica (DE-627)ELV053331885 (ELSEVIER)S0301-4622(21)00013-2 DE-627 ger DE-627 rakwb eng 610 VZ 44.87 bkl Schmidt, Thaís F. verfasserin aut Dengue fusion peptide in Langmuir monolayers: A binding parameter study 2021transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Membrane fusion is known to be the primary mechanism of entry of flaviviruses into host cells. Several studies reported the investigation of the membrane fusion mechanism mediated by the fusion peptide, a component of the membrane protein surrounding the flaviviruses. In this study, we investigated the interaction of Dengue fusion peptide (FLAg) with Langmuir monolayers to uncover the role of membrane charges and organization in its membrane binding. Binding parameters of FLAg were obtained by measuring its adsorption onto Langmuir monolayers of different types of individual lipids, as well as their mixtures. Specific peptide binding was observed in the presence of charged lipid monolayers at different pHs, revealing that the lipid composition of the membrane modulates peptide interaction, and the preference of the peptide for negatively charged lipids. Membrane fusion is known to be the primary mechanism of entry of flaviviruses into host cells. Several studies reported the investigation of the membrane fusion mechanism mediated by the fusion peptide, a component of the membrane protein surrounding the flaviviruses. In this study, we investigated the interaction of Dengue fusion peptide (FLAg) with Langmuir monolayers to uncover the role of membrane charges and organization in its membrane binding. Binding parameters of FLAg were obtained by measuring its adsorption onto Langmuir monolayers of different types of individual lipids, as well as their mixtures. Specific peptide binding was observed in the presence of charged lipid monolayers at different pHs, revealing that the lipid composition of the membrane modulates peptide interaction, and the preference of the peptide for negatively charged lipids. Riske, Karin A. oth Caseli, Luciano oth Salesse, Christian oth Enthalten in Elsevier Science Baumert, Thomas F. ELSEVIER “We can and should do better” - an interview with the 2020 Nobel prize laureates who revolutionized hepatology 2021 an international journal devoted to the physics and chemistry of biological phenomena Amsterdam [u.a.] (DE-627)ELV006315437 volume:271 year:2021 pages:0 https://doi.org/10.1016/j.bpc.2021.106553 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.87 Gastroenterologie VZ AR 271 2021 0 |
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Dengue fusion peptide in Langmuir monolayers: A binding parameter study |
| abstract |
Membrane fusion is known to be the primary mechanism of entry of flaviviruses into host cells. Several studies reported the investigation of the membrane fusion mechanism mediated by the fusion peptide, a component of the membrane protein surrounding the flaviviruses. In this study, we investigated the interaction of Dengue fusion peptide (FLAg) with Langmuir monolayers to uncover the role of membrane charges and organization in its membrane binding. Binding parameters of FLAg were obtained by measuring its adsorption onto Langmuir monolayers of different types of individual lipids, as well as their mixtures. Specific peptide binding was observed in the presence of charged lipid monolayers at different pHs, revealing that the lipid composition of the membrane modulates peptide interaction, and the preference of the peptide for negatively charged lipids. |
| abstractGer |
Membrane fusion is known to be the primary mechanism of entry of flaviviruses into host cells. Several studies reported the investigation of the membrane fusion mechanism mediated by the fusion peptide, a component of the membrane protein surrounding the flaviviruses. In this study, we investigated the interaction of Dengue fusion peptide (FLAg) with Langmuir monolayers to uncover the role of membrane charges and organization in its membrane binding. Binding parameters of FLAg were obtained by measuring its adsorption onto Langmuir monolayers of different types of individual lipids, as well as their mixtures. Specific peptide binding was observed in the presence of charged lipid monolayers at different pHs, revealing that the lipid composition of the membrane modulates peptide interaction, and the preference of the peptide for negatively charged lipids. |
| abstract_unstemmed |
Membrane fusion is known to be the primary mechanism of entry of flaviviruses into host cells. Several studies reported the investigation of the membrane fusion mechanism mediated by the fusion peptide, a component of the membrane protein surrounding the flaviviruses. In this study, we investigated the interaction of Dengue fusion peptide (FLAg) with Langmuir monolayers to uncover the role of membrane charges and organization in its membrane binding. Binding parameters of FLAg were obtained by measuring its adsorption onto Langmuir monolayers of different types of individual lipids, as well as their mixtures. Specific peptide binding was observed in the presence of charged lipid monolayers at different pHs, revealing that the lipid composition of the membrane modulates peptide interaction, and the preference of the peptide for negatively charged lipids. |
| collection_details |
GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA |
| title_short |
Dengue fusion peptide in Langmuir monolayers: A binding parameter study |
| url |
https://doi.org/10.1016/j.bpc.2021.106553 |
| remote_bool |
true |
| author2 |
Riske, Karin A. Caseli, Luciano Salesse, Christian |
| author2Str |
Riske, Karin A. Caseli, Luciano Salesse, Christian |
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ELV006315437 |
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| doi_str |
10.1016/j.bpc.2021.106553 |
| up_date |
2024-07-06T18:39:34.124Z |
| _version_ |
1803856038200344576 |
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7.402231 |