Impedance-derived electrochemical capacitance spectroscopy for the evaluation of lectin-glycoprotein binding affinity
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Data
2014-12-15
Autores
Santos, Adriano [UNESP]
Carvalho, Fernanda C. [UNESP]
Roque-Barreira, Maria-Cristina
Bueno, Paulo Roberto [UNESP]
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ISSN da Revista
Título de Volume
Editor
Elsevier B.V.
Resumo
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 proteincarbohydrate 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) x 10(8) L mol(-1). The results shown herein suggest the feasibility of ECS application for lectin glycoarray characterization. (C) 2014 Elsevier B.V. All rights reserved.
Descrição
Palavras-chave
ArtinM, HRP, Impedance-derived electrochemical capacitance spectroscopy, Langmuir isotherm, Binding affinity constant
Como citar
Biosensors & Bioelectronics. Oxford: Elsevier Advanced Technology, v. 62, p. 102-105, 2014.