Supramolecularly oriented immobilization of proteins using cucurbit[8]uril

A. González-Campo, M. Brasch, D.A. Uhlenheuer, A. Gómez-Casado, L. Yang, L. Brunsveld, J. Huskens, P. Jonkheijm

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Abstract

A supramolecular strategy is used for oriented positioning of proteins on surfaces. A viologen-based guest molecule is attached to the surface, while a naphthol guest moiety is chemoselectively ligated to a yellow fluorescent protein. Cucurbit[8]uril (CB[8]) is used to link the proteins onto surfaces through specific charge-transfer interactions between naphthol and viologen inside the CB cavity. The assembly process is characterized using fluorescence and atomic force microscopy, surface plasmon resonance, IR-reflective absorption, and X-ray photoelectron spectroscopy measurements. Two different immobilization routes are followed to form patterns of the protein ternary complexes on the surfaces. Each immobilization route consists of three steps: (i) attaching the viologen to the glass using microcontact chemistry, (ii) blocking, and (iii) either incubation or microcontact printing of CB[8] and naphthol guests. In both cases uniform and stable fluorescent patterns are fabricated with a high signal-to-noise ratio. Control experiments confirm that CB[8] serves as a selective linking unit to form stable and homogeneous ternary surface-bound complexes as envisioned. The attachment of the yellow fluorescent protein complexes is shown to be reversible and reusable for assembly as studied using fluorescence microscopy.
Original languageEnglish
Pages (from-to)16364-16371
Number of pages8
JournalLangmuir
Volume28
Issue number47
DOIs
Publication statusPublished - 2012

Fingerprint

immobilization
Viologens
Naphthols
Naphthol
proteins
Proteins
Ternary Complex Factors
assembly
routes
fluorescence
Fluorescence microscopy
Surface plasmon resonance
surface plasmon resonance
printing
positioning
attachment
Charge transfer
Printing
Atomic force microscopy
Signal to noise ratio

Cite this

González-Campo, A., Brasch, M., Uhlenheuer, D. A., Gómez-Casado, A., Yang, L., Brunsveld, L., ... Jonkheijm, P. (2012). Supramolecularly oriented immobilization of proteins using cucurbit[8]uril. Langmuir, 28(47), 16364-16371. https://doi.org/10.1021/la303987c
González-Campo, A. ; Brasch, M. ; Uhlenheuer, D.A. ; Gómez-Casado, A. ; Yang, L. ; Brunsveld, L. ; Huskens, J. ; Jonkheijm, P. / Supramolecularly oriented immobilization of proteins using cucurbit[8]uril. In: Langmuir. 2012 ; Vol. 28, No. 47. pp. 16364-16371.
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abstract = "A supramolecular strategy is used for oriented positioning of proteins on surfaces. A viologen-based guest molecule is attached to the surface, while a naphthol guest moiety is chemoselectively ligated to a yellow fluorescent protein. Cucurbit[8]uril (CB[8]) is used to link the proteins onto surfaces through specific charge-transfer interactions between naphthol and viologen inside the CB cavity. The assembly process is characterized using fluorescence and atomic force microscopy, surface plasmon resonance, IR-reflective absorption, and X-ray photoelectron spectroscopy measurements. Two different immobilization routes are followed to form patterns of the protein ternary complexes on the surfaces. Each immobilization route consists of three steps: (i) attaching the viologen to the glass using microcontact chemistry, (ii) blocking, and (iii) either incubation or microcontact printing of CB[8] and naphthol guests. In both cases uniform and stable fluorescent patterns are fabricated with a high signal-to-noise ratio. Control experiments confirm that CB[8] serves as a selective linking unit to form stable and homogeneous ternary surface-bound complexes as envisioned. The attachment of the yellow fluorescent protein complexes is shown to be reversible and reusable for assembly as studied using fluorescence microscopy.",
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González-Campo, A, Brasch, M, Uhlenheuer, DA, Gómez-Casado, A, Yang, L, Brunsveld, L, Huskens, J & Jonkheijm, P 2012, 'Supramolecularly oriented immobilization of proteins using cucurbit[8]uril', Langmuir, vol. 28, no. 47, pp. 16364-16371. https://doi.org/10.1021/la303987c

Supramolecularly oriented immobilization of proteins using cucurbit[8]uril. / González-Campo, A.; Brasch, M.; Uhlenheuer, D.A.; Gómez-Casado, A.; Yang, L.; Brunsveld, L.; Huskens, J.; Jonkheijm, P.

In: Langmuir, Vol. 28, No. 47, 2012, p. 16364-16371.

Research output: Contribution to journalArticleAcademicpeer-review

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AU - González-Campo, A.

AU - Brasch, M.

AU - Uhlenheuer, D.A.

AU - Gómez-Casado, A.

AU - Yang, L.

AU - Brunsveld, L.

AU - Huskens, J.

AU - Jonkheijm, P.

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AB - A supramolecular strategy is used for oriented positioning of proteins on surfaces. A viologen-based guest molecule is attached to the surface, while a naphthol guest moiety is chemoselectively ligated to a yellow fluorescent protein. Cucurbit[8]uril (CB[8]) is used to link the proteins onto surfaces through specific charge-transfer interactions between naphthol and viologen inside the CB cavity. The assembly process is characterized using fluorescence and atomic force microscopy, surface plasmon resonance, IR-reflective absorption, and X-ray photoelectron spectroscopy measurements. Two different immobilization routes are followed to form patterns of the protein ternary complexes on the surfaces. Each immobilization route consists of three steps: (i) attaching the viologen to the glass using microcontact chemistry, (ii) blocking, and (iii) either incubation or microcontact printing of CB[8] and naphthol guests. In both cases uniform and stable fluorescent patterns are fabricated with a high signal-to-noise ratio. Control experiments confirm that CB[8] serves as a selective linking unit to form stable and homogeneous ternary surface-bound complexes as envisioned. The attachment of the yellow fluorescent protein complexes is shown to be reversible and reusable for assembly as studied using fluorescence microscopy.

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González-Campo A, Brasch M, Uhlenheuer DA, Gómez-Casado A, Yang L, Brunsveld L et al. Supramolecularly oriented immobilization of proteins using cucurbit[8]uril. Langmuir. 2012;28(47):16364-16371. https://doi.org/10.1021/la303987c