ArticleProtein science : a publication of the Protein Society2005
Effect of hexafluoroisopropanol alcohol on the structure of melittin: a molecular dynamics simulation study.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Engineering Robust Supramolecular Nanoassemblies from Amino-Acid Functionalized Stiff-Stilbene Amphiphiles.Small science · 2026Article
- Structure-Guided Temporin L Analogs Development to Inhibit the Main Protease of SARS-CoV‑2.ACS medicinal chemistry letters · 2025Article
- Catalysis in Chemical Modification of Proteins.ChemCatChem · 2025Article
- Solvent-Dependent Chemoselectivity Switch to Arg-Lys Imidazole Cross-Links.Organic letters · 2024Article
- Article
- Examination of Solvent Interactions with Trp-Cage in 1,1,1,3,3,3-Hexafluoro-2-propanol-water at 298 K through MD Simulations and Intermolecular Nuclear Overhauser Effects.The journal of physical chemistry. B · 2023Article
- Structure of AQEE-30 of VGF Neuropeptide in Membrane-Mimicking Environments.International journal of molecular sciences · 2022Article
- Fast and selective organocatalytic ring-opening polymerization by fluorinated alcohol without a cocatalyst.Nature communications · 2019Article
- Noble Metal Composite Porous Silk Fibroin Aerogel Fibers.Materials (Basel, Switzerland) · 2019Article
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- Engineering amyloid-like assemblies from unstructured peptides via site-specific lipid conjugation.PloS one · 2014Article
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- Equilibrium and folding simulations of NS4B H2 in pure water and water/2,2,2-trifluoroethanol mixed solvent: examination of solvation models.Journal of molecular modeling · 2013Article
- Overcoming product inhibition in catalysis of the intramolecular Schmidt reaction.Journal of the American Chemical Society · 2013Article
- Deceleration of arginine kinase refolding by induced helical structures.The protein journal · 2012Article
- Large multiple transmembrane domain fragments of a G protein-coupled receptor: biosynthesis, purification, and biophysical studies.Biopolymers · 2012Article
- A multi-pronged search for a common structural motif in the secretion signal of Salmonella enterica serovar Typhimurium type III effector proteins.Molecular bioSystems · 2010Article
- Mechanisms of amphipathic helical peptide denaturation by guanidinium chloride and urea: a molecular dynamics simulation study.Journal of computer-aided molecular design · 2010Article
- Circular dichroism and UV resonance raman study of the impact of alcohols on the Gibbs free energy landscape of an alpha-helical peptide.Biochemistry · 2010Article
- Oxpholipin 11D: an anti-inflammatory peptide that binds cholesterol and oxidized phospholipids.PloS one · 2010Article
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4 authors.
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Abstract
The molecular mechanism by which HFIP stabilizes the alpha-helical structure of peptides is not well understood. In the present study, we use melittin as a model to gain insight into the details of the atomistic interactions of HFIP with the peptide. We have performed extensive comparative molecular dynamics simulations (up to 100 nsec) in the absence and in the presence of HFIP. In agreement with recent NMR experiments, the simulations show rapid loss of tertiary structure in water at pH 2 but much higher helicity in 35% HFIP. The MD simulations also indicate that melittin adopts a highly dynamic global structure in 35% HFIP solution with two alpha-helical segments sampling a wide range of angular orientations. The analysis of the HFIP distribution shows the tendency of HFIP to aggregate around the peptide, increasing the local cosolvent concentration to more than two times that in the bulk concentration. The correlation of local peptide structure with HFIP coating suggests that displacement of water at the peptide surface is the main contribution of HFIP in stabilizing the secondary structure of melittin. Finally, a stabilizing effect promoted by the presence of counter-ions was also observed in the simulations.
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