Self-assembled peptide fibers from valylvaline bola-amphiphiles by a parallel beta-sheet network.
A series of dipeptide-based bola-amphiphiles, bis(N-alpha-amide-L-valyl-L-valine) 1, n-alkane dicarboxylate (n=4-12), have been synthesized. The bola-amphiphiles with n=4 and 6 self-assembled to form crystalline solids in water, whereas those with n=7-12 produced peptide fibers. FT-IR spectroscopy and X-ray diffraction patterns revealed that the peptide fibers have parallel-type beta-sheet networks between the valylvaline units. FT-IR deconvolution study of carboxyl regions indicated that these crystalline solids and peptide fibers are stabilized by interlayer bifurcated and intralayer lateral hydrogen-bond networks between the end carboxylic acid groups, respectively.
Kogiso
M
M
National Institute of Materials and Chemical Research, 1-1 Higashi, Tsukuba, Ibaraki 305-8565, Japan. kogiso@home.nimc.go.jp
Okada
Y
Y
Hanada
T
T
Yase
K
K
Shimizu
T
T
D003460:Crystallization; D020100:Hydrogels; D006860:Hydrogen Bonding; D008854:Microscopy, Electron / Q000379:methods; D008958:Models, Molecular; D008970:Molecular Weight; D010316:Particle Size; D010455:Peptides / Q000138:chemical synthesis*; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared; D013501:Surface-Active Agents / Q000737:chemistry*; D014961:X-Ray Diffraction
D020100:Hydrogels; D010455:Peptides; D013501:Surface-Active Agents