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- W2794318150 abstract "HIV infectivity can be blocked by lipid conjugated peptides, termed lipo-peptides, which modulate various biological systems including viral fusion. These compounds have advanced the understanding of membrane protein functions and the roles of lipids in the membrane milieu. However, a single function has been suggested for the lipid, which is binding to the membrane thus elevating the peptide's local concentration at the target site. Utilizing biophysical and biochemical methods coupled with fully infectious virions we challenged this argument. We investigated the antiviral mechanism of lipo-peptides comprised of an HIV envelope derived peptide and sphinganine, the lipid backbone of dihydrosphingomyelin enriched in the HIV and target cell membrane. We uncovered a partnership that reduced CD4 diffusion and HIV-1 fusion peptide mediated lipid mixing. In addition, the lipo-peptides localized to the virus-cell and cell-cell contact sites and disrupted HIV-1 fusion protein assembly and folding. Overall, the findings might help uncover a role for elevated dihydrosphingomyelin in HIV-1 and its target cell membranes and may be implicative to lipid-protein interactions in various biological systems." @default.
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- W2794318150 date "2018-02-01" @default.
- W2794318150 modified "2023-10-13" @default.
- W2794318150 title "HIV GP41 Envelope Protein Early and Late Membrane Fusion Stages are Impaired by a Sphinganine Based Lipo-Peptide" @default.
- W2794318150 doi "https://doi.org/10.1016/j.bpj.2017.11.2531" @default.
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