Enfuvirtide is a 36 amino acid peptide corresponding to a region of gp41, the transmembrane subunit of HIV-1 envelope protein. It belongs to the therapeutic class of fusion inhibitors and acts by binding to gp41 and impeding the conformational changes in gp41 necessary for fusion of the virus with the cell.
CAT No: 10-101-14
CAS No:159519-65-0
Synonyms/Alias:T20; Pentafuside; Enfuvirtide; Fuzeon; DP178; DP-178; DP 178; HSDB 7341; HSDB7341; T-20; T 20
Chemical Name:(4S)-4-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-acetamido-3-(4-hydroxyphenyl)propanoyl]amino]-3-hydroxybutanoyl]amino]-3-hydroxypropanoyl]amino]-4-methylpentanoyl]amino]-3-methylpentanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-3-hydroxypropanoyl]amino]-4-methylpentanoyl]amino]-3-methylpentanoyl]amino]-4-carboxybutanoyl]amino]-4-carboxybutanoyl]amino]-3-hydroxypropanoyl]amino]-5-amino-5-oxopentanoyl]amino]-4-amino-4-oxobutanoyl]amino]-5-amino-5-oxopentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-5-[[(2S)-6-amino-1-[[(2S)-4-amino-1-[[(2S)-1-[[(2S)-5-amino-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-4-amino-1-[[(2S)-1-[[(2S)-1-amino-1-oxo-3-phenylpropan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-1-oxohexan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-1,5-dioxopentan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-1-oxohexan-2-yl]amino]-5-oxopentanoic acid
Enfuvirtide, also known as T-20 or Fuzeon, is a synthetic peptide that functions as a potent inhibitor of HIV-1 fusion with host cells. As a 36-amino-acid peptide derived from the HIV-1 envelope glycoprotein gp41, Enfuvirtide is engineered to disrupt the conformational changes necessary for viral entry into human cells. Its unique mechanism of action, which targets the fusion process rather than viral replication, sets it apart from other antiretroviral agents. The compound is highly valued in research settings for its specificity and ability to block HIV transmission at a crucial step in the viral lifecycle. Due to its peptide nature, Enfuvirtide is soluble in aqueous solutions and compatible with a variety of in vitro and ex vivo experimental systems. Researchers utilize this compound to explore novel antiviral strategies, investigate resistance mechanisms, and assess the molecular dynamics of viral-host interactions.
Antiviral Mechanism Studies: Enfuvirtide serves as a critical tool in elucidating the molecular mechanisms underlying viral entry inhibition. By binding to the heptad repeat region of gp41, it prevents the formation of the six-helix bundle necessary for membrane fusion. Scientists leverage this property to dissect the sequential steps of HIV-1 entry into target cells, enabling detailed mapping of protein-protein interactions and conformational changes. These insights contribute to a deeper understanding of viral pathogenesis and facilitate the identification of new targets for therapeutic intervention.
Drug Resistance Research: T-20 is indispensable in studies aimed at characterizing resistance mutations that emerge during prolonged exposure to fusion inhibitors. By applying selective pressure in cell culture models, researchers can induce and identify mutations within the gp41 region that confer reduced susceptibility to the peptide. Analysis of these resistance-associated mutations informs the design of next-generation fusion inhibitors and supports the development of combination therapies to circumvent resistance.
Viral Entry Assays: The peptide is widely employed in cell-based assays to quantify and visualize HIV-1 entry events. Its potent and specific inhibition of membrane fusion allows researchers to establish baseline controls and validate the efficacy of novel entry inhibitors. Enfuvirtide can be incorporated into fluorescence-based or luciferase reporter systems, providing robust and reproducible readouts for high-throughput screening applications. These assays are instrumental in advancing antiviral drug discovery and in the functional characterization of viral envelope proteins.
Structural Biology Investigations: Fuzeon is a valuable reagent in structural studies that aim to resolve the three-dimensional architecture of viral fusion intermediates. By stabilizing specific conformational states of gp41, it enables crystallization and cryo-electron microscopy analyses that reveal the structural basis of membrane fusion inhibition. Structural insights gained through these studies inform rational drug design and enhance the understanding of protein folding, dynamics, and function in the context of viral entry.
Peptide Engineering and Delivery Research: The synthetic nature of Enfuvirtide makes it an ideal model for investigating strategies to improve peptide stability, bioavailability, and delivery. Researchers use it to test novel formulation approaches, such as nanoparticle encapsulation or conjugation with cell-penetrating peptides, to enhance pharmacokinetic properties. These studies not only advance the field of peptide therapeutics but also provide a framework for optimizing delivery systems for a wide range of biologically active peptides.
In summary, Enfuvirtide is a cornerstone in HIV research, offering unparalleled utility in antiviral mechanism elucidation, resistance profiling, entry inhibition assays, structural biology, and peptide delivery innovation. Its application across these diverse research directions continues to drive progress in understanding viral entry processes and in the development of next-generation antiviral agents.
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