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Chemical Compound Review

TFE     2,2,2-trifluoroethanol

Synonyms: tfetoh, TFEA, Fluorinol 85, PubChem12849, NSC-451, ...
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Disease relevance of Trifluoroethanol

  • Self-association and domains of interactions of an amphipathic helix peptide inhibitor of HIV-1 integrase assessed by analytical ultracentrifugation and NMR experiments in trifluoroethanol/H(2)O mixtures [1].
  • The absorption, fluorescence, and circular dichroism properties of Escherichia coli thioredoxin, and of its tryptic fragments thioredoxin-T-(1-73) and thioredoxin-T-(74-108), in water and in trifluoroethanol, have been investigated as a function of pH and temperature in order to gain information about their conformational behavior [2].
  • In this work we present the NMR structure of the HR2 domain (residues 1141-1193) from SARS-CoV (termed S2-HR2) in the presence of the co-solvent trifluoroethanol [3].
  • To define the structural consequences of changing the amphipathic nature of GS14 analogs to maximize antimicrobial activity and to minimize hemolysis, NMR structures were determined in water and the membrane-mimetic solvent trifluoroethanol [4].
  • The antigenic activity of a 19-mer peptide corresponding to the major antigenic region of foot-and-mouth disease virus and its retro-enantiomeric analogue was found to be completely abolished when they were tested in a biosensor system in trifluoroethanol [5].

Psychiatry related information on Trifluoroethanol

  • To study the folding/unfolding properties of a beta-amyloid peptide Abeta(12-36) of Alzheimer's disease, five molecular dynamics simulations of Abeta(12-36) in explicit water were done at 450 K starting from a structure that is stable in trifluoroethanol/water at room temperature with two alpha-helices [6].

High impact information on Trifluoroethanol


Chemical compound and disease context of Trifluoroethanol


Biological context of Trifluoroethanol

  • Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol [11].
  • Based on these results we conclude that the RCC-associated t(6;11)(p21;q13) translocation leads to a dramatic transcriptional and translational upregulation of TFEB due to promoter substitution, thereby severely unbalancing the nuclear ratios of the MITF/TFE subfamily members [16].
  • The results suggest that the entropy can be an important factor for the enzyme stability, and the increase in entropy by TFE is partially responsible for the increased stability of Delta(5)-3-ketosteroid isomerase [12].
  • Molecular conformations of salmon (sCT) and human (hCT) calcitonin in media with different concentrations of methanol/water and trifluoroethanol/water have been investigated by fluorescence, circular dichroism (CD) and infrared spectroscopy techniques [17].
  • As part of this investigation we introduce (19)F, in this case from bound TFE, as a new probe for the binding of small molecules to a metalloenzyme active site [18].

Anatomical context of Trifluoroethanol

  • In the present study, we investigate the effects of 2,2,2-trifluoroethanol (TFE) on the structure of newt acidic fibroblast growth factor (nFGF-1) [19].
  • When TFE protein was produced in a rabbit reticulocyte lysate, it displayed the same specificity of DNA sequence recognition as the beta-galactosidase fusion protein and immobilization of the translation product on nitrocellulose still appeared to be essential for detecting in vitro DNA binding activity [20].
  • A series of glycosylated endorphin analogues designed to penetrate the blood-brain barrier (BBB) have been studied by circular dichroism and by 2D-NMR in the presence of water; TFE/water; SDS micelles; and in the presence of both neutral and anionic bicelles [21].
  • In naked capillaries, a buffer comprising 50 mM IDA, 10% TFE and 0.5% hydroxyethylcellulose (HEC) allows generation of peptide maps with high resolution, reduced transit times and no interaction of even large peptides with the wall [22].
  • Patch-clamp analysis of giant E. coli spheroplasts expressing MscS shows that exposure to TFE in lower concentrations (0.5-5.0 vol %) causes leftward shifts of the dose-response curves when applied extracellularly, and rightward shifts when added from the cytoplasmic side [23].

Associations of Trifluoroethanol with other chemical compounds

  • Helical structure in a series of HPLC-purified peptides was estimated from circular dichroism measurements in: 1) 0.01 M phosphate buffer, pH 7.0, 2) that buffer with 45% trifluoroethanol (TFE), and 3) that buffer with di-O-hexadecyl phosphatidylcholine vesicles [24].
  • The addition of trifluoroethanol (50% final concentration) to solutions of peptide in deionized water induced the appearance of an alpha-helical secondary structure, but did not modify the beta-sheet conformation of the peptide dissolved in 200 mM phosphate buffer, pH 5 [25].
  • The effect of trifluoroethanol and glycosaminoglycans (GAG) on the extension of the fibrils at a neutral pH was investigated with the use of fluorescence spectroscopy with thioflavin T, circular dichroism spectroscopy, and electron microscopy [26].
  • The circular dichroism study of water/trifluoroethanol (TFE) solutions of poly(dG-dC) has revealed the following: The polynucleotide is present as a B form up to a TFE content of 60% (v/v) or less [27].
  • These results indicate that, with an increase in the concentration of hydrophobic cosolvent (TFE, HFIP, or SDS), a delicate balance of decreasing hydrophobic interactions and increasing polar interactions (i.e. H-bonds) in and between peptides leads to the formation of ordered fibrils with a bell-shaped concentration dependence [28].

Gene context of Trifluoroethanol

  • Folding of the AR was observed in the presence of the helix-stabilizing solvent trifluoroethanol and the natural osmolyte trimethylamine N-oxide (TMAO) [29].
  • CD results of all analogues in 50% TFE (a concentration of TFE that induced nearly maximum helicity of [DPhe12,Nle21,38]h/rCRF12-41) suggest that while helicity may be an important factor for CRF analogue recognition, little correlation is found between percent helicity as determined by spectral deconvolution and biological activity in vitro [30].
  • The structure of the biologically-active N-terminal region of human parathyroid hormone, PTH(1-34), was investigated in the presence of 10% trifluoroethanol using two-dimensional proton NMR spectroscopy, distance geometry and dynamic simulated annealing [31].
  • To gain insight into the structure-function relationship of Vpr, (1-51)Vpr was synthesized and its structure analyzed by circular dichroism and two-dimensional 1H NMR in aqueous trifluoroethanol (30%) solution and refined by restrained molecular dynamics [32].
  • However, the motifs in Knirps and Hairy did not adopt well-defined structures in TFE/water mixtures as shown by the absence of medium range NOEs and a high proportion of signal overlap [33].

Analytical, diagnostic and therapeutic context of Trifluoroethanol

  • Protein engineering experiments on FKBP12, coupled with folding and unfolding experiments in 0% and 9.6% TFE, conclusively show that TFE does not perturb the folding pathway of this protein [34].
  • X-ray crystallography shows that this TFE domain adopts a winged helix-turn-helix (winged helix) fold, extended by specific alpha-helices at the N and C termini [35].
  • Transmission electron microscopy and x-ray fiber diffraction data show that the fibrils (induced by TFE) are straight, unbranched, and have a cross-beta structure with an average diameter of 10-15 A [19].
  • To understand the physiological mechanism of the drug delivery system, we have examined the trifluoroethanol (TFE)-induced conformational changes of the protein with special emphasis on their relation to the release of the chromophore from holoneocarzinostatin [36].
  • Cloning and sequence analysis of TFE, a helix-loop-helix transcription factor able to recognize the thyroglobulin gene promoter in vitro [20].


  1. Self-association and domains of interactions of an amphipathic helix peptide inhibitor of HIV-1 integrase assessed by analytical ultracentrifugation and NMR experiments in trifluoroethanol/H(2)O mixtures. Maroun, R.G., Krebs, D., El Antri, S., Deroussent, A., Lescot, E., Troalen, F., Porumb, H., Goldberg, M.E., Fermandjian, S. J. Biol. Chem. (1999) [Pubmed]
  2. A conformational study of thioredoxin and its tryptic fragments. Reutimann, H., Straub, B., Luisi, P.L., Holmgren, A. J. Biol. Chem. (1981) [Pubmed]
  3. Solution structure of the severe acute respiratory syndrome-coronavirus heptad repeat 2 domain in the prefusion state. Hakansson-McReynolds, S., Jiang, S., Rong, L., Caffrey, M. J. Biol. Chem. (2006) [Pubmed]
  4. Development of the structural basis for antimicrobial and hemolytic activities of peptides based on gramicidin S and design of novel analogs using NMR spectroscopy. McInnes, C., Kondejewski, L.H., Hodges, R.S., Sykes, B.D. J. Biol. Chem. (2000) [Pubmed]
  5. Solution structure of a retro-inverso peptide analogue mimicking the foot-and-mouth disease virus major antigenic site. Structural basis for its antigenic cross-reactivity with the parent peptide. Petit, M.C., Benkirane, N., Guichard, G., Du, A.P., Marraud, M., Cung, M.T., Briand, J.P., Muller, S. J. Biol. Chem. (1999) [Pubmed]
  6. General dynamic properties of Abeta12-36 amyloid peptide involved in Alzheimer's disease from unfolding simulation. Suzuki, S., Galzitskaya, O.V., Mitomo, D., Higo, J. J. Biochem. (2004) [Pubmed]
  7. A chemically synthesized Antennapedia homeo domain binds to a specific DNA sequence. Mihara, H., Kaiser, E.T. Science (1988) [Pubmed]
  8. Melanocytes and the microphthalmia transcription factor network. Steingrímsson, E., Copeland, N.G., Jenkins, N.A. Annu. Rev. Genet. (2004) [Pubmed]
  9. Mutational analysis of the propensity for amyloid formation by a globular protein. Chiti, F., Taddei, N., Bucciantini, M., White, P., Ramponi, G., Dobson, C.M. EMBO J. (2000) [Pubmed]
  10. Total chemical synthesis and electrophysiological characterization of mechanosensitive channels from Escherichia coli and Mycobacterium tuberculosis. Clayton, D., Shapovalov, G., Maurer, J.A., Dougherty, D.A., Lester, H.A., Kochendoerfer, G.G. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  11. Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol. Hamada, D., Chiti, F., Guijarro, J.I., Kataoka, M., Taddei, N., Dobson, C.M. Nat. Struct. Biol. (2000) [Pubmed]
  12. Trifluoroethanol increases the stability of Delta(5)-3-ketosteroid isomerase. 15N NMR relaxation studies. Yun, S., Jang, d.o. .S., Choi, G., Kim, K.S., Choi, K.Y., Lee, H.C. J. Biol. Chem. (2002) [Pubmed]
  13. Structures of revertant signal sequences of Escherichia coli ribose binding protein. Chi, S.W., Yi, G.S., Suh, J.Y., Choi, B.S., Kim, H. Biophys. J. (1995) [Pubmed]
  14. Metabolism of 2,2,2-trifluoroethanol and its relationship to toxicity. Fraser, J.M., Kaminsky, L.S. Toxicol. Appl. Pharmacol. (1987) [Pubmed]
  15. 2,2,2-Trifluoroethanol intestinal and bone marrow toxicity: the role of its metabolism to 2,2,2-trifluoroacetaldehyde and trifluoroacetic acid. Fraser, J.M., Kaminsky, L.S. Toxicol. Appl. Pharmacol. (1988) [Pubmed]
  16. Upregulation of the transcription factor TFEB in t(6;11)(p21;q13)-positive renal cell carcinomas due to promoter substitution. Kuiper, R.P., Schepens, M., Thijssen, J., van Asseldonk, M., van den Berg, E., Bridge, J., Schuuring, E., Schoenmakers, E.F., van Kessel, A.G. Hum. Mol. Genet. (2003) [Pubmed]
  17. Comparative study of human and salmon calcitonin secondary structure in solutions with low dielectric constants. Arvinte, T., Drake, A.F. J. Biol. Chem. (1993) [Pubmed]
  18. Product binding to the diiron(III) and mixed-valence diiron centers of methane monooxygenase hydroxylase studied by (1,2)H and (19)F ENDOR spectroscopy. Smoukov, S.K., Kopp, D.A., Valentine, A.M., Davydov, R., Lippard, S.J., Hoffman, B.M. J. Am. Chem. Soc. (2002) [Pubmed]
  19. Amyloid-like fibril formation in an all beta-barrel protein. Partially structured intermediate state(s) is a precursor for fibril formation. Srisailam, S., Kumar, T.K., Rajalingam, D., Kathir, K.M., Sheu, H.S., Jan, F.J., Chao, P.C., Yu, C. J. Biol. Chem. (2003) [Pubmed]
  20. Cloning and sequence analysis of TFE, a helix-loop-helix transcription factor able to recognize the thyroglobulin gene promoter in vitro. Javaux, F., Donda, A., Vassart, G., Christophe, D. Nucleic Acids Res. (1991) [Pubmed]
  21. Glycopeptides related to beta-endorphin adopt helical amphipathic conformations in the presence of lipid bilayers. Dhanasekaran, M., Palian, M.M., Alves, I., Yeomans, L., Keyari, C.M., Davis, P., Bilsky, E.J., Egleton, R.D., Yamamura, H.I., Jacobsen, N.E., Tollin, G., Hruby, V.J., Porreca, F., Polt, R. J. Am. Chem. Soc. (2005) [Pubmed]
  22. Generation of peptide maps by capillary zone electrophoresis in isoelectric iminodiacetic acid. Bossi, A., Righetti, P.G. Electrophoresis (1997) [Pubmed]
  23. 2,2,2-Trifluoroethanol Changes the Transition Kinetics and Subunit Interactions in the Small Bacterial Mechanosensitive Channel MscS. Akitake, B., Spelbrink, R.E., Anishkin, A., Killian, J.A., de Kruijff, B., Sukharev, S. Biophys. J. (2007) [Pubmed]
  24. Role of recurrent hydrophobic residues in catalysis of helix formation by T cell-presented peptides in the presence of lipid vesicles. Lu, S., Reyes, V.E., Lew, R.A., Anderson, J., Mole, J., Humphreys, R.E., Ciardelli, T. J. Immunol. (1990) [Pubmed]
  25. Conformational polymorphism of the amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. De Gioia, L., Selvaggini, C., Ghibaudi, E., Diomede, L., Bugiani, O., Forloni, G., Tagliavini, F., Salmona, M. J. Biol. Chem. (1994) [Pubmed]
  26. Glycosaminoglycans enhance the trifluoroethanol-induced extension of beta 2-microglobulin-related amyloid fibrils at a neutral pH. Yamamoto, S., Yamaguchi, I., Hasegawa, K., Tsutsumi, S., Goto, Y., Gejyo, F., Naiki, H. J. Am. Soc. Nephrol. (2004) [Pubmed]
  27. The transitions between left- and right-handed forms of poly(dG-dC). Ivanov, V.I., Minyat, E.E. Nucleic Acids Res. (1981) [Pubmed]
  28. Mechanism by Which the Amyloid-like Fibrils of a beta(2)-Microglobulin Fragment Are Induced by Fluorine-substituted Alcohols. Yamaguchi, K., Naiki, H., Goto, Y. J. Mol. Biol. (2006) [Pubmed]
  29. Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions. Reid, J., Kelly, S.M., Watt, K., Price, N.C., McEwan, I.J. J. Biol. Chem. (2002) [Pubmed]
  30. Conformationally restricted competitive antagonists of human/rat corticotropin-releasing factor. Miranda, A., Koerber, S.C., Gulyas, J., Lahrichi, S.L., Craig, A.G., Corrigan, A., Hagler, A., Rivier, C., Vale, W., Rivier, J. J. Med. Chem. (1994) [Pubmed]
  31. Stabilized NMR structure of human parathyroid hormone(1-34). Barden, J.A., Cuthbertson, R.M. Eur. J. Biochem. (1993) [Pubmed]
  32. NMR structure of the (1-51) N-terminal domain of the HIV-1 regulatory protein Vpr. Wecker, K., Roques, B.P. Eur. J. Biochem. (1999) [Pubmed]
  33. Structural determinants outside the PXDLS sequence affect the interaction of adenovirus E1A, C-terminal interacting protein and Drosophila repressors with C-terminal binding protein. Molloy, D.P., Barral, P.M., Bremner, K.H., Gallimore, P.H., Grand, R.J. Biochim. Biophys. Acta (2001) [Pubmed]
  34. Does trifluoroethanol affect folding pathways and can it be used as a probe of structure in transition states? Main, E.R., Jackson, S.E. Nat. Struct. Biol. (1999) [Pubmed]
  35. An extended winged helix domain in general transcription factor E/IIE alpha. Meinhart, A., Blobel, J., Cramer, P. J. Biol. Chem. (2003) [Pubmed]
  36. Release of the neocarzinostatin chromophore from the holoprotein does not require major conformational change of the tertiary and secondary structures induced by trifluoroethanol. Sudhahar, G.C., Balamurugan, K., Chin, D.H. J. Biol. Chem. (2000) [Pubmed]
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