A revised indirect mechanism is proposed for the effect of 2,2,2- trifluoroethanol on peptide conformation (TFE effect) that suggest tighter solvent shells in pure water for helical states than random coil states. The alcoholic cosolvent stabilizes the helical state preferentially by disrupting the solvent shell, which causes unfavorable enthalpic and favorable entropic contributions to the free energy of helix formation. This revised mechanism was adapted because it best explained the solvent-dependent thermodynamic behavior of the coil/helix transition. To define the TFE effect, solvent- dependent physicochemical behaviors of two molecular probes for solvent character were monitored and compared with the solvent dependence of peptide helix formation. The rate of decarboxylations of 6-nitro-3- carboxybenzisoxazole was determined in aqueous mixtures as a function of concentration for DMSO, EtOH, MeOH, (i)PrOH, HFIP, and TFE. To relate these rate studies to the cosolvent-dependent thermodynamics of helix formation, ΔH(±) and ΔS(±) as a function of concentration for EtOH and TFE were determined and interpreted. The mixed solvent dependence of the UV spectrum of a solvatochromic ketone was also monitored to correlate the behavior of the mixed solvent systems with a microscopic polarity index.
|Number of pages||7|
|Journal||Journal of the American Chemical Society|
|State||Published - May 27 1998|
ASJC Scopus subject areas
- Chemistry (all)
- Colloid and Surface Chemistry