Dengue fusion peptide in Langmuir monolayers: A binding parameter study

Biophys Chem. 2021 Apr:271:106553. doi: 10.1016/j.bpc.2021.106553. Epub 2021 Feb 4.

Abstract

Membrane fusion is known to be the primary mechanism of entry of flaviviruses into host cells. Several studies reported the investigation of the membrane fusion mechanism mediated by the fusion peptide, a component of the membrane protein surrounding the flaviviruses. In this study, we investigated the interaction of Dengue fusion peptide (FLAg) with Langmuir monolayers to uncover the role of membrane charges and organization in its membrane binding. Binding parameters of FLAg were obtained by measuring its adsorption onto Langmuir monolayers of different types of individual lipids, as well as their mixtures. Specific peptide binding was observed in the presence of charged lipid monolayers at different pHs, revealing that the lipid composition of the membrane modulates peptide interaction, and the preference of the peptide for negatively charged lipids.

Keywords: Binding parameters; Dengue virus; Fusion peptide; Langmuir monolayers; Phospholipids.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Dengue Virus / chemistry*
  • Lipids / chemistry*
  • Viral Fusion Proteins / chemistry*

Substances

  • Lipids
  • Viral Fusion Proteins