ArticleEuropean biophysics journal : EBJ2011
Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.
Article in European biophysics journal : EBJ, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 41 citations in OpenAlex.
- A Frame-by-Frame Glance at Membrane Fusion Mechanisms: From Viral Infections to Fertilization.Biomolecules · 2023Review
- Structures Controlled by Entropy: The Flexibility of Strychnine as Example.Molecules (Basel, Switzerland) · 2022Article
- Computational methods to study enveloped viral entry.Biochemical Society transactions · 2021Review
- Configuration determination by residual dipolar couplings: accessing the full conformational space by molecular dynamics with tensorial constraints.Chemical science · 2019Article
- Nano-biomimetic carriers are implicated in mechanistic evaluation of intracellular gene delivery.Scientific reports · 2017Article
- Homo- and heteromeric interaction strengths of the synergistic antimicrobial peptides PGLa and magainin 2 in membranes.European biophysics journal : EBJ · 2016Article
- Magic angle spinning NMR of viruses.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- Hydrophobic mismatch demonstrated for membranolytic peptides, and their use as molecular rulers to measure bilayer thickness in native cells.Scientific reports · 2015Article
- The three lives of viral fusion peptides.Chemistry and physics of lipids · 2014Review
- Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel β sheet fusion peptide structure in the final six-helix bundle state.Journal of molecular biology · 2014Article
- Structure analysis and conformational transitions of the cell penetrating peptide transportan 10 in the membrane-bound state.PloS one · 2014Article
- A GxxxG-like motif within HIV-1 fusion peptide is critical to its immunosuppressant activity, structure, and interaction with the transmembrane domain of the T-cell receptor.The Journal of biological chemistry · 2012Article
- Computer-Aided Approaches for Targeting HIVgp41.Biology · 2012Article
- Membrane-active peptides and the clustering of anionic lipids.Biophysical journal · 2012Article
- Antimicrobial and cell-penetrating peptides induce lipid vesicle fusion by folding and aggregation.European biophysics journal : EBJ · 2012Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To better understand peptide-induced membrane fusion at a molecular level, we set out to determine the structure of the fusogenic peptide FP23 from the HIV-1 protein gp41 when bound to a lipid bilayer. An established solid-state (19)F nuclear magnetic resonance (NMR) approach was used to collect local orientational constraints from a series of CF(3)-phenylglycine-labeled peptide analogues in macroscopically aligned membranes. Fusion assays showed that these (19)F-labels did not significantly affect peptide function. The NMR spectra were characteristic of well-behaved samples, without any signs of heterogeneity or peptide aggregation at 1:300 in 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine (DMPC). We can conclude from these NMR data that FP23 has a well-defined (time-averaged) conformation and undergoes lateral diffusion in the bilayer plane, presumably as a monomer or small oligomer. Attempts to evaluate its conformation in terms of various secondary structures, however, showed that FP23 does not form any type of regular helix or β-strand. Therefore, all-atom molecular dynamics (MD) simulations were carried out using the orientational NMR constraints as pseudo-forces to drive the peptide into a stable alignment and structure. The resulting picture suggests that FP23 can adopt multiple β-turns and insert obliquely into the membrane. Such irregular conformation explains why the structure of the fusion peptide could not be reliably determined by any biophysical method so far.
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