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• W2732012045 startingPage "56" @default.
• W2732012045 abstract "Non-structural NS2A protein of Dengue virus is essential for viral replication but poorly characterized because of its high hydrophobicity. We have previously shown experimentally that NS2A possess a segment, peptide dens25, known to insert into membranes and interact specifically with negatively-charged phospholipids. To characterize its membrane interaction we have used two types of molecular dynamics membrane model systems, a highly mobile membrane mimetic (HMMM) and an endoplasmic reticulum (ER) membrane-like model. Using the HMMM system, we have been able of demonstrating the spontaneous binding of dens25 to the negatively-charged phospholipid 1,2-divaleryl-sn-glycero-3-phosphate containing membrane whereas no binding was observed for the membrane containing the zwitterionic one 1,2-divaleryl-sn-glycero-3-phosphocholine. Using the ER-like membrane model system, we demonstrate the spontaneous insertion of dens25 into the middle of the membrane, it maintained its three-dimensional structure and presented a nearly parallel orientation with respect to the membrane surface. Both charged and hydrophobic amino acids, presenting an interfacial/hydrophobic pattern characteristic of a membrane-proximal segment, are responsible for membrane binding and insertion. Dens25 might control protein/membrane interaction and be involved in membrane rearrangements critical for the viral cycle. These data should help us in the development of inhibitor molecules that target NS2A segments involved in membrane reorganisation." @default.
• W2732012045 created "2017-07-14" @default.
• W2732012045 creator A5014499518 @default.
• W2732012045 creator A5054470710 @default.
• W2732012045 creator A5070546071 @default.
• W2732012045 date "2017-08-01" @default.
• W2732012045 modified "2023-09-24" @default.
• W2732012045 title "Spontaneous membrane insertion of a dengue virus NS2A peptide" @default.
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• W2732012045 doi "https://doi.org/10.1016/j.abb.2017.06.016" @default.
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