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Modulation of protein behavior through light responses of TiO(2) nanodots films

In this work, the behavior of protein molecules adsorbed on TiO(2) nanodots films are modulated through the light responses of the nanodots. TiO(2) nanodots films are first prepared through phase separation induced self assembly. Then, bovine serum albumin (BSA) is adsorbed on TiO(2) nanodots films...

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Detalles Bibliográficos
Autores principales: Cheng, Kui, Hong, Yi, Yu, Mengfei, Lin, Jun, Weng, Wenjian, Wang, Huiming
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4549798/
https://www.ncbi.nlm.nih.gov/pubmed/26306638
http://dx.doi.org/10.1038/srep13354
Descripción
Sumario:In this work, the behavior of protein molecules adsorbed on TiO(2) nanodots films are modulated through the light responses of the nanodots. TiO(2) nanodots films are first prepared through phase separation induced self assembly. Then, bovine serum albumin (BSA) is adsorbed on TiO(2) nanodots films and exposed to ultraviolet (365 nm) illumination. It is found the conformation of surface-bound BSA molecules changes with ultraviolet illumination. Moreover, the BSA molecules conjugate to the surface-bound molecules, which are in the overlayer, are released. The reason is ascribed to that TiO(2) nanodots absorb ultraviolet and result in the increase of surface hydroxyl groups on nanodots. Such increase further leads to intensified attraction of -NH3 groups in the surface-bound BSA molecules. That not only changes the conformation of the surface-bound BSA molecules, but also weaken the conjugation between surface-bound molecules and other BSA molecules in the overlayer. Eventually, the overlayer of BSA molecules is released. It is believed that such protein conformation variation and release behavior induced through light responses of TiO(2) nanodots are crucial in understanding the biomedical performance of TiO(2) nanostructures. Also, it could be widely utilized in tailoring of the materials-protein interactions.