Conformational Diversity of the Fibrillogenic Fusion Peptide B18 in Different Environments from Molecular Dynamics Simulations

2007 ◽  
Vol 111 (16) ◽  
pp. 4161-4170 ◽  
Author(s):  
Volker Knecht ◽  
Helmut Möhwald ◽  
Reinhard Lipowsky
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Fusion Peptide ◽  
Conformational Diversity ◽  
Dynamics Simulations

scholarly journals Effect of pH on the influenza fusion peptide properties unveiled by constant-pH molecular dynamics simulations combined with experiment

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Diana Lousa ◽  
Antónia R. T. Pinto ◽  
Sara R. R. Campos ◽  
António M. Baptista ◽  
Ana S. Veiga ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Genetic Material ◽  
Fusion Peptide ◽  
Terminal Region ◽  
Constant Ph ◽  
Large Conformational Change ◽  
Membrane Spanning ◽  
Dynamics Simulations ◽  
Constant Ph Molecular Dynamics

AbstractThe influenza virus fusion process, whereby the virus fuses its envelope with the host endosome membrane to release the genetic material, takes place in the acidic late endosome environment. Acidification triggers a large conformational change in the fusion protein, hemagglutinin (HA), which enables the insertion of the N-terminal region of the HA2 subunit, known as the fusion peptide, into the membrane of the host endosome. However, the mechanism by which pH modulates the molecular properties of the fusion peptide remains unclear. To answer this question, we performed the first constant-pH molecular dynamics simulations of the influenza fusion peptide in a membrane, extending for 40 µs of aggregated time. The simulations were combined with spectroscopic data, which showed that the peptide is twofold more active in promoting lipid mixing of model membranes at pH 5 than at pH 7.4. The realistic treatment of protonation introduced by the constant-pH molecular dynamics simulations revealed that low pH stabilizes a vertical membrane-spanning conformation and leads to more frequent contacts between the fusion peptide and the lipid headgroups, which may explain the increase in activity. The study also revealed that the N-terminal region is determinant for the peptide’s effect on the membrane.

Stability of SIV gp32 Fusion-Peptide Single-Layer Protofibrils as Monitored by Molecular-Dynamics Simulations

2005 ◽  
Vol 117 (7) ◽  
pp. 1089-1091 ◽  
Author(s):  
Patricia Soto ◽  
Josep Cladera ◽  
Alan E. Mark ◽  
Xavier Daura
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Single Layer ◽  
Fusion Peptide ◽  
Dynamics Simulations
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