@article{oai:kyutech.repo.nii.ac.jp:00005298,
 author = {Arai,  Toru and Imachi,  Takashi and Kato, Tamaki and 加藤, 珠樹 and Nishino, Norikazu and 西野, 憲和},
 issue = {2},
 journal = {Bulletin of the Chemical Society of Japan},
 month = {Feb},
 note = {Amphiphilic 21-peptides with six and nine L-2-(2,2,2-trifluoroethyl)glycines as the hydrophobic amino acids and lysine and glutamic acid as the hydrophilic amino acids were synthesized. The CD spectra showed that these peptides with　L-2-(2,2,2-trifluoroethyl)glycines took a random conformation in H2O. On the contrary, similar amphiphilic 21-peptides with leucine as the hydrophobic amino acids took a helical conformation in H2O. The peptides with L-2-(2,2,2-trifluoroethyl)glycines took a helical conformation in H2O containing a > 20% volume of 2,2,2-trifluoroethanol. These facts suggested the hydrophobic nature of the L-trifluoroethylglycines. The peptide with six L-2-(2,2,2-trifluoroethyl)glycines took a helical structure in methanol, however it slowly changed into the β-structure within 24 h. Interestingly, the peptide with nine L-2-(2,2,2-trifluoroethyl)glycines formed a stable helix under the same conditions. The peptide with nine L-2-(2,2,2-trifluoroethyl)glycines preferred a helical structure, probably because the assembling of the Tfeg side chains was more effective in forming its helix rather than the β-structure.},
 pages = {439--445},
 title = {The Conformation of de Novo Designed Amphiphilic Peptides with Six or Nine L-2-(2,2,2-Trifluoroethyl)glycines as the Hydrophobic Amino Acid},
 volume = {73},
 year = {2000},
 yomi = {カトウ, タマキ and ニシノ, ノリカズ}
}