Antiviral Lipopeptide-Cell Membrane Interaction Is Influenced by PEG Linker Length.
| Autor: | Augusto MT; Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Av. Prof. Egas Moniz, 1649-028 Lisboa, Portugal. maugusto@fm.ul.pt., Hollmann A; Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Av. Prof. Egas Moniz, 1649-028 Lisboa, Portugal. ahollmann@medicina.ulisboa.pt.; Laboratory of Molecular Microbiology, Institute of Basic and Applied Microbiology, National University of Quilmes, Roque Sáenz Peña N° 352, Bernal, 1876 Buenos Aires, Argentina. ahollmann@medicina.ulisboa.pt.; Laboratory of Biointerfaces and Biomimetic Systems, CITSE, National University of Santiago del Estero-CONICET, 4200 Santiago del Estero, Argentina. ahollmann@medicina.ulisboa.pt., Porotto M; Center for Host-Pathogen Interaction, Columbia University Medical Center, 701 W. 168th, New York, NY 10032, USA. mp3509@cumc.columbia.edu.; Department of Pediatrics, Columbia University Medical Center, 701 W. 168th, New York, NY 10032, USA. mp3509@cumc.columbia.edu., Moscona A; Center for Host-Pathogen Interaction, Columbia University Medical Center, 701 W. 168th, New York, NY 10032, USA. am939@cumc.columbia.edu.; Department of Pediatrics, Columbia University Medical Center, 701 W. 168th, New York, NY 10032, USA. am939@cumc.columbia.edu.; Department of Microbiology & Immunology, Columbia University Medical Center, 701 W. 168th, New York, NY 10032, USA. am939@cumc.columbia.edu.; Department of Physiology & Cellular Biophysics, Columbia University Medical Center, 701 W. 168th, New York, NY 10032, USA. am939@cumc.columbia.edu., Santos NC; Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Av. Prof. Egas Moniz, 1649-028 Lisboa, Portugal. nsantos@fm.ul.pt. |
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| Jazyk: | angličtina |
| Zdroj: | Molecules (Basel, Switzerland) [Molecules] 2017 Jul 15; Vol. 22 (7). Date of Electronic Publication: 2017 Jul 15. |
| DOI: | 10.3390/molecules22071190 |
| Abstrakt: | A set of lipopeptides was recently reported for their broad-spectrum antiviral activity against viruses belonging to the Paramyxoviridae family, including human parainfluenza virus type 3 and Nipah virus. Among them, the peptide with a 24-unit PEG linker connecting it to a cholesterol moiety (VG-PEG24-Chol) was found to be the best membrane fusion inhibitory peptide. Here, we evaluated the interaction of the same set of peptides with biomembrane model systems and isolated human peripheral blood mononuclear cells (PBMC). VG-PEG24-Chol showed the highest insertion rate and it was among the peptides that induced a larger change on the surface pressure of cholesterol rich membranes. This peptide also displayed a high affinity towards PBMC membranes. These data provide new information about the dynamics of peptide-membrane interactions of a specific group of antiviral peptides, known for their potential as multipotent paramyxovirus antivirals. Competing Interests: The authors declare no conflict of interest. |
| Databáze: | MEDLINE |
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