Contact
    Start Publications Unsaturated Lipid Accelerates Formation of Oligomeric ...
    ←  Publication Finder
    KSV NIMA

    Unsaturated Lipid Accelerates Formation of Oligomeric beta-Sheet Structure of GP41 Fusion Peptide in Model Cell Membrane

    Year: 2020

    Journal: J. Phys. Chem. B, Volume 124, JUN 25, page 5169–5176

    Authors: Wang, WT; Tan, JJ; Ye, SJ

    Organizations: National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [21925302, 21633007, 21873090]; National Key Research and Development Program of China [2018YFA0208700, 2017YFA0303500]; Anhui Initiative in Quantum Information Technologies [AHY090000]

    Membrane fusion of the viral and host cell membranes is the initial step of virus infection and is catalyzed by fusion peptides. Although the beta-sheet structure of fusion peptides has been proposed to be the most important fusion-active conformation, it is still very challenging to experimentally identify different types of beta-sheet structures at the cell membrane surface in situ and in real time. In this work, we demonstrate that the interface-sensitive amide II spectral signals of protein backbones, generated by the sum frequency generation vibrational spectroscopy, provide a sensitive probe for directly capturing the formation of oligomeric beta-sheet structure of fusion peptides. Using human immunodeficiency virus (HIV) glycoprotein GP41 fusing peptide (FP23) as the model, we find that formation speed of oligomeric beta-sheet structure depends on lipid unsaturation. The unsaturated lipid such as POPG can accelerate formation of oligomeric beta-sheet structure of FP23. The beta-sheet structure is more deeply inserted into the hydrophobic region of the POPG bilayer than the a-helical segment. This work will pave the way for future researches on capturing intermediate structures during membrane fusion processes and revealing the fusion mechanism.
    View publication