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Fabrication of Reversible Poly(dimethylsiloxane) Surfaces via Host–Guest Chemistry and Their Repeated Utilization in Cardiac Biomarker Analysis

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posted on 22.02.2016, 11:29 by Yanrong Zhang, Li Ren, Qin Tu, Xueqin Wang, Rui Liu, Li Li, Jian-Chun Wang, Wenming Liu, Juan Xu, Jinyi Wang
On the basis of the host–guest interactions between azobenzenes and cyclodextrins, a new strategy for the preparation of a dually functionalized poly(dimethylsiloxane) (PDMS) surface was investigated using surface-initiated atom-transfer radical polymerization (SI-ATRP) and click chemistry. The PDMS substrates were first oxidized in a H2SO4/H2O2 solution to transform the surface Si–CH3 groups into Si–OH groups. Then, the SI-ATRP initiator 3-(2-bromoisobutyramido)propyl(trime-thoxy)silane was grafted onto the substrates through a silanization reaction. Sequentially, the poly(ethylene glycol) (PEG) units were introduced onto the PDMS–Br surfaces via SI-ATRP reaction using oligo(ethylene glycol) methacrylate. Afterward, the bromide groups on the surface were converted to azido groups via nucleophilic substitution reaction with NaN3. Finally, the azido-grafted PDMS surfaces were subjected to a click reaction with alkynyl and PEG-modified β-cyclodextrins, resulting in the grafting of cyclodextrins onto the PDMS surfaces. The composition and chemical state of the modified surfaces were characterized via X-ray photoelectron spectroscopy, and the stability and dynamic characteristics of the cyclodextrin-modified PDMS substrates were investigated via attenuated total reflection-Fourier transform infrared spectroscopy and temporal contact angle experiments. The surface morphology of the modified PDMS surfaces was characterized through imaging using a multimode atomic force microscope. A protein adsorption assay using Alexa Fluor594-labeled bovine serum albumin, Alexa Fluor594-labeled chicken egg albumin, and FITC-labeled lysozyme shows that the prepared PDMS surfaces possess good protein-repelling properties. On-surface studies on the interactions between azobenzenes and the cyclodextrin-modified surfaces reveal that the reversible binding of azobenzene to the cyclodextrin-modified PDMS surfaces and its subsequent release can be reversibly controlled using UV irradiation. Sandwich fluoroimmunoassay of the cardiac markers myoglobin and fatty acid-binding protein demonstrates that the cyclodextrin-modified PDMS surfaces can be repeatedly utilized in disease biomarker analysis.

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