Double assembly composed of lectin association with columnar molecular assembly of cyclic tri-beta-peptide having sugar units.
A novel double assembly was prepared by association between a columnar molecular assembly of cyclic tri-beta-peptides having sugar units and lectins. The NMR, FT-IR, and circular dichroism (CD) spectroscopy as well as computational calculations revealed that this compound took a flat and C3 symmetrical conformation and that the amide N-H and C=O groups protruded vertically to the ring plane. This disk-shaped molecule stacked one by one to form a columnar structure via intermolecular hydrogen bonds between the amide groups. WGA lectin moderately bound to this columnar assembly to form a double assembly. Another lectin (Con A) disturbed the columnar structure upon strong binding, and RCA lectin showed no binding. Fluorescence spectroscopy revealed that the association between WGA lectin and columnar assembly of cyclic glycopeptide could be achieved due to the high density of the hydroxyl groups on the assembly surface (cluster effects). Interestingly, after cross-linking the lectins bound to the columnar assembly (the double assembly) by glutaraldehyde, the core column of cyclic tri-beta-peptides could be washed away to leave the protein nanotube.
Fujimura
Futoshi
F
Department of Material Chemistry, Graduate School of Engineering, Kyoto University, Kyoto-Daigaku-Katsura, Nishikyo-ku, Kyoto 615-8510, Japan.
Horikawa
Yoshiki
Y
Morita
Tomoyuki
T
Sugiyama
Junji
J
Kimura
Shunsaku
S
D006860:Hydrogen Bonding; D037102:Lectins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008968:Molecular Conformation; D043942:Nanotubes / Q000737:chemistry*; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000378:metabolism; D013057:Spectrum Analysis
D037102:Lectins; D010456:Peptides, Cyclic