Abstract
Reported herein are the design, biological activities, and biophysical properties of a novel HIV-1 membrane fusion inhibitor. alpha-Helix-inducible X-EE-XX-KK motifs were applied to design an enfuvirtide analogue 2 that exhibited highly potent anti-HIV activity against wild-type HIV-1, enfuvirtide-resistant HIV-1 strains, and an HIV-2 strain in vitro. Indispensable residues for bioactivity of enfuvirtide, including the residues interacting with the N-terminal heptad repeat and the C-terminal hydrophobic residues, were identified.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Drug Resistance, Viral
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Enfuvirtide
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HIV Envelope Protein gp41 / chemical synthesis*
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HIV Envelope Protein gp41 / chemistry
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HIV Envelope Protein gp41 / pharmacology
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HIV Fusion Inhibitors / chemical synthesis*
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HIV Fusion Inhibitors / chemistry
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HIV Fusion Inhibitors / pharmacology
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HIV-1 / drug effects*
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HIV-1 / physiology
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Molecular Sequence Data
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Peptide Fragments / chemical synthesis*
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Peptide Fragments / chemistry
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Peptide Fragments / pharmacology
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Protein Binding
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Protein Structure, Secondary
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Structure-Activity Relationship
Substances
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HIV Envelope Protein gp41
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HIV Fusion Inhibitors
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Peptide Fragments
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Enfuvirtide