ArticleProceedings of the National Academy of Sciences of the United States of America2002
Mechanism by which 2,2,2-trifluoroethanol/water mixtures stabilize secondary-structure formation in peptides: a molecular dynamics study.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 136 papers.
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136 citing papers in PubMed.
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- Study of the Myosin Relay Helix Peptide by Molecular Dynamics Simulations, Pump-Probe and 2D Infrared Spectroscopy.International journal of molecular sciences · 2024Article
- Foldamers controlled by functional triamino acids: structural investigation of α/γ-hybrid oligopeptides.Communications chemistry · 2024Article
- Dual-Capped Helical Interface Mimics.Journal of the American Chemical Society · 2024Article
- Antimicrobial Peptide-Poly(ethylene glycol) Conjugates: Connecting Molecular Architecture, Solution Properties, and Functional Performance.ACS polymers Au · 2024Article
- Insights into the Adsorption Mechanisms of the Antimicrobial Peptide CIDEM-501 on Membrane Models.Antibiotics (Basel, Switzerland) · 2024Article
76 more citing papers are in PubMed but not listed here.
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4 authors.
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Abstract
Molecular dynamics simulation techniques have been used to investigate the effect of 2,2,2-trifluoroethanol (TFE) as a cosolvent on the stability of three different secondary structure-forming peptides: the alpha-helix from Melittin, the three-stranded beta-sheet peptide Betanova, and the beta-hairpin 41-56 from the B1 domain of protein G. The peptides were studied in pure water and 30% (vol/vol) TFE/water mixtures at 300 K. The simulations suggest that the stabilizing effect of TFE is induced by the preferential aggregation of TFE molecules around the peptides. This coating displaces water, thereby removing alternative hydrogen-bonding partners and providing a low dielectric environment that favors the formation of intrapeptide hydrogen bonds. Because TFE interacts only weakly with nonpolar residues, hydrophobic interactions within the peptides are not disrupted. As a consequence, TFE promotes stability rather than inducing denaturation.
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