Glycosylated aniline polymer sensor: amine to imine conversion on protein-carbohydrate binding.
Glycosylated aniline polymer sensor: amine to imine conversion on protein-carbohydrate binding.
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DOI:
10.1016/j.bios.2013.02.030
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发表时间:
2013-08-15
影响因子:
12.6
通讯作者:
Zeng, Xiangqun
中科院分区:
文献类型:
--
作者:
Wang, Zhe;Sun, Chunyan;Vegesna, Giri;Liu, Haiying;Liu, Yang;Li, Jinghong;Zeng, Xiangqun
In this report, functionalized mannosylated aniline polymer (manno-PANI) was investigated as an electrochemical platform to study carbohydrate–protein interactions by exploiting the conductivity change of manno-PANI when the specific lectin binding occurs. A systematic study was performed to characterize the interconversion of polyaniline content (from amine to imine) in manno-PANI by UV–vis spectroscopy during its binding with concanavalin A (Con A). Both X-ray photoelectron spectrometry (XPS) and UV–vis results suggest that Con A binding with the manno-PANI film triggers the switching of amine functionalities in the polyaniline backbone, converting them to imine forms. Electrochemical impedance spectroscopy (EIS) was used to quantify the specific interactions between Con A and mannose by measuring the impedance change of manno-PANI film for the detection of Con A. A linear relationship between the impedance and Con A concentration was obtained, and the detection limit reaches to 0.12 nM Con A in a buffer solution (pH=7.4), whereas the addition of nonspecific control lectins to the same manno-PANI film gave very little impedance variations. Stability characterization of the manno-PANI film over 20 weeks shows a maximum drift of only 3% from the original signal. Thus, the uniquely constructed carbohydrate–PANI hybrid is a promising new carbohydrate recognition moiety for studying carbohydrate-protein interactions, presumably leading to a new electrochemical method for characterization of carbohydrate–protein interactions and carbohydrate-mediated intercellular recognitions.
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