期刊
BIOPHYSICAL CHEMISTRY
卷 271, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.bpc.2021.106553
关键词
Dengue virus; Fusion peptide; Langmuir monolayers; Binding parameters; Phospholipids
资金
- FAPESP [2013/23096-3]
- Natural Sciences and Engineering Research Council of Canada (NSERC)
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [BEPE 2015/10057-5]
The study explored the interaction of Dengue fusion peptide (FLAg) with Langmuir monolayers, revealing that the lipid composition modulates peptide binding, with a preference for negatively charged lipids.
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.
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