185385-99-3Relevant academic research and scientific papers
Photosensitive azopolymer brushes via atom transfer radical polymerization for protein sensing
Zhang, Zhihong,Wang, Yaoyan,Yan, Fufeng,Peng, Donglai,Ma, Zhi
, p. 153 - 158 (2011)
Novel photosensitive azopolymer brushes were synthesized via surface initiated atom transfer radical polymerization using initiator self-assembled on Au surface. The chemical structures of azobenzene derivatives were confirmed by Fourier transform infrared spectroscopy (FTIR) and nuclear magnetic resonance spectroscopy (NMR). The surface morphology of azopolymers via atom transfer radical polymerization (ATRP) for different time was investigated by atomic force microscopy (AFM). Additionally, the photoisomerization of azopolymer was measured by ultraviolet-visible spectroscopy (UV-Vis). The results indicate that such azopolymers can undergo trans-cis-trans photoisomerization efficiently by photo-irradiation with UV light. Furthermore, this photoisomerization property could also induce the reversible adsorption of bovine serum albumin (BSA) adsorption on azopolymer brush surfaces. This adsorption kinetics of the reversible process can be measured by surface plasmon resonance (SPR) spectroscopy in situ. It suggests that the protein biochips could be regenerated safely by UV irradiation rather than by being rinsed with chemical reagents. Novel photosensitive azopolymer brushes were synthesized via surface initiated atom transfer radical polymerization using initiator self-assembled on Au surface. Such azopolymers can undergo trans-cis-trans photoisomerization efficiently by photo-irradiation with UV light. It could lead to the reversible adsorption of bovine serum albumin (BSA) adsorption on azopolymer brush surfaces. It suggests that the protein biochips could be regenerated safely by UV irradiation rather than by being rinsed with chemical reagents. This photodeformable surface on the azopolymer warrants further investigation for protein chip application since the azopolymer can hold protein molecules without denaturation caused by one-step photoirradiation. Copyright
