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• W2100049032 endingPage "13430" @default.
• W2100049032 startingPage "13426" @default.
• W2100049032 abstract "Linear peptides derived from the membrane proximal region of the gp41 ectodomain are effective inhibitors of HIV type 1 (HIV-1)-mediated fusion events. These inhibitory peptides lack structure in solution, rendering mechanistic interpretation of their activity difficult. Using structurally constrained analogs of these molecules, we demonstrate that the peptides inhibit infectivity by adopting a helical conformation. Moreover, we show that a specific face of the helix must be exposed to block viral infectivity. Recent crystal structures show that the region of gp41 corresponding to the inhibitory peptides is helical and uses the analogous face to pack against a groove formed by an N-terminal coiled-coil trimer. Our results provide a direct link between the inhibition of HIV-1 infectivity by these peptides and the x-ray structures, and suggest that the conformation of gp41 observed by crystallography represents the fusogenic state. Other agents that block HIV-1 infectivity by binding to this groove may hold promise for the treatment of AIDS." @default.
• W2100049032 created "2016-06-24" @default.
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• W2100049032 date "1997-12-09" @default.
• W2100049032 modified "2023-09-25" @default.
• W2100049032 title "Inhibition of HIV type 1 infectivity by constrained α-helical peptides: Implications for the viral fusion mechanism" @default.
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• W2100049032 doi "https://doi.org/10.1073/pnas.94.25.13426" @default.
• W2100049032 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/28321" @default.
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• W2100049032 hasPublicationYear "1997" @default.
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