Solid state NMR measurements of conformation and conformational distributions in the membrane-bound HIV-1 fusion peptide

Jun Yang, Paul D. Parkanzky, Bhagyashree A. Khunte, Christian G. Canlas, Rong Yang, Charles M. Gabrys, David P. Weliky*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    23 Scopus citations


    The solid state NMR lineshape of a protein backbone carbonyl nucleus is a general diagnostic of the local conformational distribution in the vicinity of that nucleus. In addition, measurements of carbonyl chemical shifts and 2D exchange spectra provide information about the most probable conformation in the distribution. These types of solid state NMR methodologies have been applied to structural studies of the membrane-bound HIV-1 fusion peptide. This peptide is derived from a domain of the HIV-1 gp41 envelope protein, which is critical for viral-host cell-membrane fusion. Even in the absence of the rest of the envelope protein, the fusion peptide will fuse liposomes or erythrocytes. The solid state NMR measurements demonstrate that the center of the membrane-bound HIV-1 fusion peptide is structured, while the C-terminus is highly disordered. The structural distribution at the peptide center is lipid-dependent, with the greatest degree of structural homogeneity in a lipid environment whose composition reflects that of the target T cells. When bound to the lipid mixture, the peptide center is predominately β sheet. The β-sheet structure may be diagnostic of peptide oligomerization, which is thought to be a requirement for membrane fusion activity. Although the peptide partially disrupts bilayer orientational ordering in stacked glass-plate samples, 2H NMR demonstrates that the bilayers remain intact in the presence of the fusion peptide and are not micellized. The retention of the bilayer phase may relate to the biological requirement that the virus should fuse with, but not destroy, the target host cell membrane.

    Original languageEnglish (US)
    Pages (from-to)129-135
    Number of pages7
    JournalJournal of Molecular Graphics and Modelling
    Issue number1
    StatePublished - 2001

    Bibliographical note

    Funding Information:
    D.P.W. acknowledges support from Michigan State University and from a Camille and Henry Dreyfus Foundation New Faculty Award.


    • 2D exchange
    • AIDS
    • Chemical shift
    • Fusion peptide
    • HIV-1
    • Magic angle spinning
    • Membrane fusion
    • NMR
    • Solid state NMR

    ASJC Scopus subject areas

    • Spectroscopy
    • Physical and Theoretical Chemistry
    • Computer Graphics and Computer-Aided Design
    • Materials Chemistry


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