基于阻抗的电化学电容谱法评价凝集素-糖蛋白结合亲和力。
Impedance-derived electrochemical capacitance spectroscopy for the evaluation of lectin-glycoprotein binding affinity.
机构信息
Department of Physical Chemistry, Chemistry Institute, São Paulo State University (Unesp), 55 Prof. Francisco Degni Street, ZIP Code: 14800-060, São Paulo, Brazil.
Department of Cellular and Molecular Biology and Pathogenic Bioagents, Ribeirão Preto Medical School. University of São Paulo (USP), 3900 Bandeirantes Avenue. ZIP Code: 14049-900, Ribeirão Preto, São Paulo, Brazil.
出版信息
Biosens Bioelectron. 2014 Dec 15;62:102-5. doi: 10.1016/j.bios.2014.06.034. Epub 2014 Jun 20.
Characterization of lectin-carbohydrate binding using label-free methods such as impedance-derived electrochemical capacitance spectroscopy (ECS) is desirable to evaluate specific interactions, for example, ArtinM lectin and horseradish peroxidase (HRP) glycoprotein, used here as a model for protein-carbohydrate binding affinity. An electroactive molecular film comprising alkyl ferrocene as a redox probe and ArtinM as a carbohydrate receptive center to target HRP was successfully used to determine the binding affinity between ArtinM and HRP. The redox capacitance, a transducer signal associated with the alkyl ferrocene centers, was obtained by ECS and used in the Langmuir adsorption model to obtain the affinity constant (1.6±0.6)×10(8) L mol(-1). The results shown herein suggest the feasibility of ECS application for lectin glycoarray characterization.
使用无标记方法（如基于阻抗的电化学电容谱（ECS））来表征凝集素-碳水化合物的结合是理想的，可用于评估特定的相互作用，例如，这里使用 ArtinM 凝集素和辣根过氧化物酶（HRP）糖蛋白作为蛋白质-碳水化合物结合亲和力的模型。成功地使用包含烷基二茂铁作为氧化还原探针和 ArtinM 作为碳水化合物受体中心以靶向 HRP 的电化学生分子膜来确定 ArtinM 和 HRP 之间的结合亲和力。通过 ECS 获得与烷基二茂铁中心相关的传导体信号的氧化还原电容，并将其用于 Langmuir 吸附模型中以获得亲和常数（1.6±0.6）×10(8) L mol(-1)。本文的结果表明，ECS 应用于凝集素糖阵列表征是可行的。
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