Responsive Photonic Crystal Carbohydrate Hydrogel Sensor Materials for Selective and Sensitive Lectin Protein Detection

被引:88
作者
Cai, Zhongyu [1 ]
Sasmal, Aniruddha [1 ]
Liu, Xinyu [1 ]
Asher, Sanford A. [1 ]
机构
[1] Univ Pittsburgh, Dept Chem, Pittsburgh, PA 15260 USA
关键词
photonic crystals; carbohydrate hydrogels; biosensors; lectin proteins detection; copolymerization; BINDING; RICIN; GLYCONANOPARTICLES; NANOPARTICLES; SPECIFICITY; FLUORESCENT; DIFFRACTION; FABRICATION; BIOSENSOR; GALACTOSE;
D O I
10.1021/acssensors.7b00426
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Lectin proteins, such as the highly toxic lectin protein, ricin, and the immunochemically important lectin, jacalin, play significant roles in many biological functions. It is highly desirable to develop a simple but efficient method to selectively detect lectin proteins. Here we report the development of carbohydrate containing responsive hydrogel sensing materials for the selective detection of lectin proteins. The copolymerization of a vinyl linked carbohydrate monomer with acrylamide and acrylic acid forms a carbohydrate hydrogel that shows specific "multivalent" binding to lectin proteins. The resulting carbohydrate hydrogels are attached to 2-D photonic crystals (PCs) that brightly diffract visible light. This diffraction provides an optical readout that sensitively monitors the hydrogel volume. We utilize lactose, galactose, and mannose containing hydrogels to fabricate a series of 2-D PC sensors that show strong selective binding to the lectin proteins ricin, jacalin, and concanavalin A (Con A). This binding causes a carbohydrate hydrogel shrinkage which significantly shifts the diffraction wavelength. The resulting 2-D PC sensors can selectively detect the lectin proteins ricin, jacalin, and Con A. These unoptimized 2-D PC hydrogel sensors show a limit of detection (LoD) of 7.5 X 10(-8)M for ricin, a LoD of 2.3 X 10(-7) M for jacalin, and a LoD of 3.8 X 10(-8) M for Con A, respectively. This sensor fabrication approach may enable numerous sensors for the selective detection of numerous lectin proteins.
引用
收藏
页码:1474 / 1481
页数:8
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