"Threading" of beta-sheet peptides via radical polymerization.
A nonamer peptide containing a diene group in the center of the sequence was synthesized. When the peptide forms an antiparallel beta-sheet, the diene groups align ca. 5 A apart on the beta-sheet. The diene groups successfully photopolymerized without distorting the beta-sheet structure. The obtained beta-sheet showed high stability against acid denaturation and addition of 1,1,1,3,3,3-hexafluoroisopropanol.
Mori
Takeshi
T
Department of Applied Chemistry and Center for Future Chemistry, Kyushu University, 744 Motooka Nishi-ku, Fukuoka 819-0395, Japan. moritcm@mbox.nc.kyushu-u.ac.jp
Yasutake
Shiro
S
Inoue
Hideki
H
Minagawa
Keiji
K
Tanaka
Masami
M
Niidome
Takuro
T
Katayama
Yoshiki
Y
D000466:Alkadienes; D010455:Peptides / Q000737:chemistry*; D010777:Photochemistry; D020005:Propanols; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D006845:Hydrocarbons, Fluorinated
D000466:Alkadienes; D010455:Peptides; D020005:Propanols; C001337:hexafluoroisopropanol; D006845:Hydrocarbons, Fluorinated