Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7233237 | Biosensors and Bioelectronics | 2014 | 4 Pages |
Abstract
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)Ã108 L molâ1. The results shown herein suggest the feasibility of ECS application for lectin glycoarray characterization.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Adriano Santos, Fernanda C. Carvalho, Maria-Cristina Roque-Barreira, Paulo R. Bueno,