ArticleBiophysical journal2008
Free-energy profiles of membrane insertion of the M2 transmembrane peptide from influenza A virus.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Vectorial insertion of a β-helical peptide into membrane: a theoretical study on polytheonamide B.Biophysical journal · 2021Article
- A novel chemical biology and computational approach to expedite the discovery of new-generation polymyxins against life-threateningChemical science · 2021Article
- COVID-19: insights into virus-receptor interactions.Molecular biomedicine · 2021Article
- Quantitative Characterization of Protein-Lipid Interactions by Free Energy Simulation between Binary Bilayers.Journal of chemical theory and computation · 2019Article
- Computed Free Energies of Peptide Insertion into Bilayers are Independent of Computational Method.The Journal of membrane biology · 2018Article
- Recent theoretical and computational advances for modeling protein-ligand binding affinities.Advances in protein chemistry and structural biology · 2011Review
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Authors and funding
4 authors.
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Abstract
The insertion of the M2 transmembrane peptide from influenza A virus into a membrane has been studied with molecular-dynamics simulations. This system is modeled by an atomically detailed peptide interacting with a continuum representation of a membrane bilayer in aqueous solution. We performed replica-exchange molecular-dynamics simulations with umbrella-sampling techniques to characterize the probability distribution and conformation preference of the peptide in the solution, at the membrane interface, and in the membrane. The minimum in the calculated free-energy surface of peptide insertion corresponds to a fully inserted, helical peptide spanning the membrane. The free-energy profile also shows that there is a significant barrier for the peptide to enter into this minimum in a nonhelical conformation. The sequence of the peptide is such that hydrophilic amino acid residues at the ends of the otherwise primarily hydrophobic peptide create a trapped, U-shaped conformation with the hydrophilic residues associated with the aqueous phase and the hydrophobic residues embedded in the membrane. Analysis of the free energy shows that the barrier to insertion is largely enthalpic in nature, whereas the membrane-spanning global minimum is favored by entropy.
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