Aromatic Functionality of Target Proteins Influences Monomer Selection for Creating Artificial Antibodies on Plasmonic Biosensors.
Aromatic Functionality of Target Proteins Influences Monomer Selection for Creating Artificial Antibodies on Plasmonic Biosensors.
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DOI：
10.1021/acsami.6b12505
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发表时间：
2017-01-11
影响因子：
9.5
通讯作者：
Morrissey JJ
中科院分区：
文献类型：
--
作者：
Hu R;Luan J;Kharasch ED;Singamaneni S;Morrissey JJ
用作生物识别元件的天然抗体具有许多缺点，例如有限的化学和环境稳定性以及成本。基于分子印迹的人工抗体是天然抗体的一种有吸引力的替代品。我们研究了芳香族相互作用在人工抗体的靶标识别能力中的作用。以三种芳香族氨基酸含量不同的蛋白质为模型靶。使用不同芳香族官能度的硅烷单体的组合在纳米结构上形成人工抗体。我们采用等离子体纳米结构的折射率敏感性作为转导平台，用于监测印迹过程中的各个步骤，并量化人工抗体的靶标识别能力。具有芳香相互作用的人工抗体的灵敏度表现出蛋白依赖性增强。由于芳香族基团的存在下，印迹聚合物基质中的选择性和灵敏度增强被认为是较高的芳香族氨基酸含量的目标蛋白质。我们的研究结果表明，基于目标蛋白的氨基酸含量定制单体组成可以提高基于人工抗体的等离子体生物传感器的灵敏度，而不影响选择性。
Natural antibodies used as biorecognition elements suffer from numerous shortcomings, such as limited chemical and environmental stability and cost. Artificial antibodies based on molecular imprinting are an attractive alternative to natural antibodies. We investigated the role of aromatic interactions in target recognition capabilities of artificial antibodies. Three proteins with different aromatic amino acid content were employed as model targets. Artificial antibodies were formed on nanostructures using combinations of silane monomers of varying aromatic functionality. We employed refractive index sensitivity of plasmonic nanostruc-tures as a transduction platform for monitoring various steps in the imprinting process and to quantify the target recognition capabilities of the artificial antibodies. The sensitivity of the artificial antibodies with aromatic interactions exhibited a protein-dependent enhancement. Selectivity and sensitivity enhancement due to the presence of aromatic groups in imprinted polymer matrix was found to be higher for target proteins with higher aromatic amino acid content. Our results indicate that tailoring the monomer composition based on the amino acid content of the target protein can improve the sensitivity of plasmonic biosensors based on artificial antibodies without affecting the selectivity.