Reversible and oriented immobilization of ferrocene-modified proteins

Lanti Yang, A. Gomez Casado, Jacqui F. Young, Hoang D. Nguyen, Jordi Cabanas Danés, Jurriaan Huskens, Luc Brunsveld, Pascal Jonkheijm

Research output: Contribution to journalArticleAcademicpeer-review

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Abstract

Adopting supramolecular chemistry for immobilization of proteins is an attractive strategy that entails reversibility and responsiveness to stimuli. The reversible and oriented immobilization and micropatterning of ferrocene-tagged yellow fluorescent proteins (Fc-YFPs) onto β-cyclodextrin (βCD) molecular printboards was characterized using surface plasmon resonance (SPR) spectroscopy and fluorescence microscopy in combination with electrochemistry. The proteins were assembled on the surface through the specific supramolecular host–guest interaction between βCD and ferrocene. Application of a dynamic covalent disulfide lock between two YFP proteins resulted in a switch from monovalent to divalent ferrocene interactions with the βCD surface, yielding a more stable protein immobilization. The SPR titration data for the protein immobilization were fitted to a 1:1 Langmuir-type model, yielding KLM = 2.5 × 105 M–1 and Ki,s = 1.2 × 103 M–1, which compares favorably to the intrinsic binding constant presented in the literature for the monovalent interaction of ferrocene with βCD self-assembled monolayers. In addition, the SPR binding experiments were qualitatively simulated, confirming the binding of Fc-YFP in both divalent and monovalent fashion to the βCD monolayers. The Fc-YFPs could be patterned on βCD surfaces in uniform monolayers, as revealed using fluorescence microscopy and atomic force microscopy measurements. Both fluorescence microscopy imaging and SPR measurements were carried out with the in situ capability to perform cyclic voltammetry and chronoamperometry. These studies emphasize the repetitive desorption and adsorption of the ferrocene-tagged proteins from the βCD surface upon electrochemical oxidation and reduction, respectively
Original languageEnglish
Pages (from-to)19199-19206
Number of pages8
JournalJournal of the American Chemical Society
Volume134
Issue number46
DOIs
Publication statusPublished - 2012

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Cyclodextrins
Immobilization
Proteins
Surface Plasmon Resonance
Surface plasmon resonance
Fluorescence microscopy
Fluorescence Microscopy
Monolayers
Electrochemistry
Supramolecular chemistry
Atomic Force Microscopy
Optical Imaging
Chronoamperometry
ferrocene
Electrochemical oxidation
Disulfides
Self assembled monolayers
Adsorption
Oxidation-Reduction
Titration

Keywords

  • METIS-293815
  • IR-85057

Cite this

Yang, L., Gomez Casado, A., Young, J. F., Nguyen, H. D., Cabanas Danés, J., Huskens, J., ... Jonkheijm, P. (2012). Reversible and oriented immobilization of ferrocene-modified proteins. Journal of the American Chemical Society, 134(46), 19199-19206. https://doi.org/10.1021/ja308450n
Yang, Lanti ; Gomez Casado, A. ; Young, Jacqui F. ; Nguyen, Hoang D. ; Cabanas Danés, Jordi ; Huskens, Jurriaan ; Brunsveld, Luc ; Jonkheijm, Pascal. / Reversible and oriented immobilization of ferrocene-modified proteins. In: Journal of the American Chemical Society. 2012 ; Vol. 134, No. 46. pp. 19199-19206.
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abstract = "Adopting supramolecular chemistry for immobilization of proteins is an attractive strategy that entails reversibility and responsiveness to stimuli. The reversible and oriented immobilization and micropatterning of ferrocene-tagged yellow fluorescent proteins (Fc-YFPs) onto β-cyclodextrin (βCD) molecular printboards was characterized using surface plasmon resonance (SPR) spectroscopy and fluorescence microscopy in combination with electrochemistry. The proteins were assembled on the surface through the specific supramolecular host–guest interaction between βCD and ferrocene. Application of a dynamic covalent disulfide lock between two YFP proteins resulted in a switch from monovalent to divalent ferrocene interactions with the βCD surface, yielding a more stable protein immobilization. The SPR titration data for the protein immobilization were fitted to a 1:1 Langmuir-type model, yielding KLM = 2.5 × 105 M–1 and Ki,s = 1.2 × 103 M–1, which compares favorably to the intrinsic binding constant presented in the literature for the monovalent interaction of ferrocene with βCD self-assembled monolayers. In addition, the SPR binding experiments were qualitatively simulated, confirming the binding of Fc-YFP in both divalent and monovalent fashion to the βCD monolayers. The Fc-YFPs could be patterned on βCD surfaces in uniform monolayers, as revealed using fluorescence microscopy and atomic force microscopy measurements. Both fluorescence microscopy imaging and SPR measurements were carried out with the in situ capability to perform cyclic voltammetry and chronoamperometry. These studies emphasize the repetitive desorption and adsorption of the ferrocene-tagged proteins from the βCD surface upon electrochemical oxidation and reduction, respectively",
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Yang, L, Gomez Casado, A, Young, JF, Nguyen, HD, Cabanas Danés, J, Huskens, J, Brunsveld, L & Jonkheijm, P 2012, 'Reversible and oriented immobilization of ferrocene-modified proteins' Journal of the American Chemical Society, vol. 134, no. 46, pp. 19199-19206. https://doi.org/10.1021/ja308450n

Reversible and oriented immobilization of ferrocene-modified proteins. / Yang, Lanti; Gomez Casado, A.; Young, Jacqui F.; Nguyen, Hoang D.; Cabanas Danés, Jordi; Huskens, Jurriaan; Brunsveld, Luc; Jonkheijm, Pascal.

In: Journal of the American Chemical Society, Vol. 134, No. 46, 2012, p. 19199-19206.

Research output: Contribution to journalArticleAcademicpeer-review

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T1 - Reversible and oriented immobilization of ferrocene-modified proteins

AU - Yang, Lanti

AU - Gomez Casado, A.

AU - Young, Jacqui F.

AU - Nguyen, Hoang D.

AU - Cabanas Danés, Jordi

AU - Huskens, Jurriaan

AU - Brunsveld, Luc

AU - Jonkheijm, Pascal

PY - 2012

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N2 - Adopting supramolecular chemistry for immobilization of proteins is an attractive strategy that entails reversibility and responsiveness to stimuli. The reversible and oriented immobilization and micropatterning of ferrocene-tagged yellow fluorescent proteins (Fc-YFPs) onto β-cyclodextrin (βCD) molecular printboards was characterized using surface plasmon resonance (SPR) spectroscopy and fluorescence microscopy in combination with electrochemistry. The proteins were assembled on the surface through the specific supramolecular host–guest interaction between βCD and ferrocene. Application of a dynamic covalent disulfide lock between two YFP proteins resulted in a switch from monovalent to divalent ferrocene interactions with the βCD surface, yielding a more stable protein immobilization. The SPR titration data for the protein immobilization were fitted to a 1:1 Langmuir-type model, yielding KLM = 2.5 × 105 M–1 and Ki,s = 1.2 × 103 M–1, which compares favorably to the intrinsic binding constant presented in the literature for the monovalent interaction of ferrocene with βCD self-assembled monolayers. In addition, the SPR binding experiments were qualitatively simulated, confirming the binding of Fc-YFP in both divalent and monovalent fashion to the βCD monolayers. The Fc-YFPs could be patterned on βCD surfaces in uniform monolayers, as revealed using fluorescence microscopy and atomic force microscopy measurements. Both fluorescence microscopy imaging and SPR measurements were carried out with the in situ capability to perform cyclic voltammetry and chronoamperometry. These studies emphasize the repetitive desorption and adsorption of the ferrocene-tagged proteins from the βCD surface upon electrochemical oxidation and reduction, respectively

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KW - IR-85057

U2 - 10.1021/ja308450n

DO - 10.1021/ja308450n

M3 - Article

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EP - 19206

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

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