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• W2090198596 abstract "Influenza virus hemagglutinin (HA)-mediated membrane fusion involves insertion into target membranes of a stretch of amino acids located at the N-terminus of the HA2 subunit of HA at low pH. The pKa of the α-amino group of 1Gly of the fusion peptide was measured using 15N NMR. The pKa of this group was found to be 8.69 in the presence of DOPC (1,2-dioleoyl-sn-glycero-3-phosphocholine). The high value of this pKa is indicative of stabilization of the protonated form of the amine group through noncovalent interactions. The shift reagent Pr3+ had large effects on the 15N resonance from the α-amino group of Gly1 of the fusion peptide in DOPC vesicles, indicating that the terminal amino group was exposed to the bulk solvent, even at low pH. Furthermore, electron paramagnetic resonance studies on the fusion peptide region of spin-labeled derivatives of a larger HA construct are consistent with the N-terminus of this peptide being at the depth of the phosphate headgroups. We conclude that at both neutral and acidic pH, the N-terminal of the fusion peptide is close to the aqueous phase and is protonated. Thus neither a change in the state of ionization nor a significant increase in membrane insertion of this group is associated with increased fusogenicity at low pH." @default.
• W2090198596 created "2016-06-24" @default.
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• W2090198596 date "2000-05-01" @default.
• W2090198596 modified "2023-10-17" @default.
• W2090198596 title "15N NMR Study of the Ionization Properties of the Influenza Virus Fusion Peptide in Zwitterionic Phospholipid Dispersions" @default.
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• W2090198596 doi "https://doi.org/10.1016/s0006-3495(00)76785-3" @default.
• W2090198596 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1300830" @default.
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