Alpha-helix formation in melittin and beta-lactoglobulin A induced by fluorinated dialcohols.

Extensive study of the effect of fluorinated alcohols on protein conformations, notably the induction of alpha-helix formation, is important because of its wide range of applications. Circular dichroism (CD) was used to show that the enhancement of helix induction in beta-lactoglobulin A and melittin by the fluorinated diols 2,2,3,3-tetrafluoro-1,4-butanediol (TFBD), 2,2,3,3,4,4-hexafluoro-1,6-pentanediol (HFPD), and 2,2,3,3,4,4,5,5-octafluoro-1,6-hexanediol (OFHD) increases in the order TFBD < HFPD < OFHD. For fluorinated diols and monoalcohols the effectiveness of helix induction was found to increase exponentially with increasing number of fluorine atoms per alcohol molecule, and OFHD was found to be more effective than any previously reported fluorinated alcohol. Formation of standard micelles was ruled out as the cause of the enhanced helix induction by the fluorinated diols. The negligible red-edge excitation shift in the fluorescence of melittin indicated that the fluorinated diol/water solvent shell surrounding the tryptophan chromophore is less immobilized than are molecules in a lamellar vesicle.