Predicting the right spacing between protein immobilization sites on self-assembled monolayers to optimize ligand binding

Javier Batista Perez, Deependra Tyagi, Mo Yang, Loany Calvo, Rolando Perez, Ernesto Moreno, Jinsong Zhu

Producción científica: Contribución a una revistaArtículorevisión exhaustiva

1 Cita (Scopus)

Resumen

Abstract Self-assembled monolayers designed to immobilize capture antibodies are usually prepared using a mixture of functional and inactive linkers. Here, using low molar ratios (1:1 to 1:100) of the two linkers resulted in loss of binding capability of the anti-EGFR (epidermal growth factor receptor) antibody nimotuzumab, as assessed by surface plasmon resonance imaging. We then developed a simple theoretical model to predict the optimal surface density of the functional linker, taking into account the antibody size and linker diameter. A high (1:1000) dilution of the functional linker yielded the best results. As an advantage, this approach does not require chemical modification of the protein.

Idioma originalInglés
Número de artículo12078
Páginas (desde-hasta)133-135
Número de páginas3
PublicaciónAnalytical Biochemistry
Volumen484
DOI
EstadoPublicada - 24 jun. 2015
Publicado de forma externa

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