Fujita Seiya, Matsuura Kazunori
Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Tottori, 680-8552, Japan.
Org Biomol Chem. 2017 Jun 14;15(23):5070-5077. doi: 10.1039/c7ob00998d.
In order to construct artificial viral capsids bearing complementary dimeric coiled-coils on the surface, a β-annulus peptide bearing a coiled-coil forming sequence at the C-terminus (β-annulus-coiled-coil-B) was synthesized by a native chemical ligation of a β-annulus-SBn peptide with a Cys-containing coiled-coil-B peptide. Dynamic light scattering (DLS) measurements and transmission electron microscopy (TEM) images revealed that the β-annulus-coiled-coil-B peptide self-assembled into spherical structures of about 50 nm in 10 mM Tris-HCl buffer. Circular dichroism (CD) spectra indicated the formation of the complementary coiled-coil structure on the spherical assemblies. Addition of 0.25 equivalent of the complementary coiled-coil-A peptide to the β-annulus-coiled-coil-B peptide showed the formation of spherical assemblies of 46 ± 14 nm with grains of 5 nm at the surface, whereas addition of 1 equivalent of the complementary coiled-coil-A peptide generated fibrous assemblies.
为了构建表面带有互补二聚卷曲螺旋的人工病毒衣壳，通过将β-环肽-SBn肽与含半胱氨酸的卷曲螺旋-B肽进行天然化学连接，合成了一种在C端带有卷曲螺旋形成序列的β-环肽（β-环-卷曲螺旋-B）。动态光散射（DLS）测量和透射电子显微镜（TEM）图像显示，β-环-卷曲螺旋-B肽在10 mM Tris-HCl缓冲液中自组装成约50 nm的球形结构。圆二色性（CD）光谱表明在球形组装体上形成了互补的卷曲螺旋结构。向β-环-卷曲螺旋-B肽中加入0.25当量的互补卷曲螺旋-A肽，形成了表面有5 nm颗粒的46±14 nm球形组装体，而加入1当量的互补卷曲螺旋-A肽则产生纤维状组装体。
