Terpyridine-based organic-inorganic hybrid nanofiber and its application as an adsorbent for protein.
A terpyridine-based organic-inorganic hybrid amphiphile possessing a triethoxylsilane moiety was synthesized and following its self-assembly in the presence of Cu2+ ion, its binding ability of histidine and His-tag proteins was observed by UV-VIS spectroscopy, Circular dichroism spectroscopy and confocal fluorescence microscopy. The self-assembled 1 in the absence and the presence Cu2+ ion revealed a helical fiber structure, and the self-assembled 1 formed a 1:1 complex with Cu2+ ion. Histidine bound to the self-assembled 1-Cu2+ ion, but more interestingly, His-tag protein was selectively bound to the surface of the self-assembled 1-Cu2+ nanofiber. The finding indicates that the self-assembled 1-Cu2+ nanofiber selectively recognized the His-tag protein.
Department of Chemistry and Research Institute of Natural Science, Gyeongsang National University, Jinju 660-701, Korea.
Doo Ri
DR
Bae
Eun Jin
EJ
Cho
Jeong Ku
JK
Kang
Jong Hwa
JH
Jung
D000327:Adsorption; D003300:Copper / Q000737:chemistry; D006639:Histidine / Q000737:chemistry / Q000378:metabolism; D018613:Microscopy, Confocal; D008855:Microscopy, Electron, Scanning; D046529:Microscopy, Electron, Transmission; D053761:Nanocomposites / Q000737:chemistry*; D057139:Nanofibers / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D011725:Pyridines / Q000737:chemistry* / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry* / Q000378:metabolism
C471213:His-His-His-His-His-His; D009842:Oligopeptides; D011725:Pyridines; D011994:Recombinant Proteins; D006639:Histidine; D003300:Copper