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• W2313198121 abstract "We have synthesized a small library of 38 variants of the 23-residue fusion peptide domain found at the N-terminus of gp41 glycoprotein of HIV. This hydrophobic, glycine-rich sequence is critical for viral infectivity and is thought to be central in the membrane fusion of viral envelope with the host membrane. There has been extensive discussion regarding the origin of fusogenicity in this viral fusion sequence. Our library of fusion peptide variants was designed to address the biophysical importance of secondary structure, peptide flexibility, glycine content, and placement. We assayed each peptide for its ability to induce lipid mixing and membrane permeablization in synthetic vesicles. We find that the viral fusion peptide may be greatly simplified while retaining fusogenic function and minimizing membrane-permeablizing function; to the best of our knowledge, this is the first attempt to optimize fusogenic function of the HIV fusion peptide through sequence variation. Our data show that many flexible, linear, minimally hydrophobic peptides may achieve the biophysical function of fusion; glycine does not appear to be essential. These findings will be useful in the design of synthetic fusogens for cellular delivery." @default.
• W2313198121 created "2016-06-24" @default.
• W2313198121 creator A5064558120 @default.
• W2313198121 creator A5067894634 @default.
• W2313198121 date "2011-05-20" @default.
• W2313198121 modified "2023-09-25" @default.
• W2313198121 title "Determinants of Membrane Activity from Mutational Analysis of the HIV Fusion Peptide" @default.
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• W2313198121 doi "https://doi.org/10.1021/bi200696s" @default.
• W2313198121 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21561063" @default.
• W2313198121 hasPublicationYear "2011" @default.
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