Directed Supramolecular Surface Assembly of SNAP-tag Fusion Proteins

D.A. Uhlenheuer, D. Wasserberg, C. Haase, Hoang D. Nguyen, J.H. Schenkel, Jurriaan Huskens, B.J. Ravoo, Pascal Jonkheijm, Luc Brunsveld

Research output: Contribution to journalArticleAcademicpeer-review

34 Citations (Scopus)

Abstract

Supramolecular assembly of proteins on surfaces and vesicles was investigated by site-selective incorporation of a supramolecular guest element on proteins. Fluorescent proteins were site-selectively labeled with bisadamantane by SNAP-tag technology. The assembly of the bisadamantane functionalized SNAP-fusion proteins on cyclodextrin-coated surfaces yielded stable monolayers. The binding of the fusion proteins is specific and occurs with an affinity in the order of 106 M−1 as determined by surface plasmon resonance. Reversible micropatterns of the fusion proteins on micropatterned cyclodextrin surfaces were visualized by using fluorescence microscopy. Furthermore, the guest-functionalized proteins could be assembled out of solution specifically onto the surface of cyclodextrin vesicles. The SNAP-tag labeling of proteins thus allows for assembly of modified proteins through a host–guest interaction on different surfaces. This provides a new strategy in fabricating protein patterns on surfaces and takes advantage of the high labeling efficiency of the SNAP-tag with designed supramolecular elements
Original languageUndefined
Pages (from-to)6788-6794
Number of pages7
JournalChemistry: a European journal
Volume18
Issue number22
DOIs
Publication statusPublished - 2012

Keywords

  • METIS-289517
  • IR-84737

Cite this

Uhlenheuer, D. A., Wasserberg, D., Haase, C., Nguyen, H. D., Schenkel, J. H., Huskens, J., ... Brunsveld, L. (2012). Directed Supramolecular Surface Assembly of SNAP-tag Fusion Proteins. Chemistry: a European journal, 18(22), 6788-6794. https://doi.org/10.1002/chem.201200238
Uhlenheuer, D.A. ; Wasserberg, D. ; Haase, C. ; Nguyen, Hoang D. ; Schenkel, J.H. ; Huskens, Jurriaan ; Ravoo, B.J. ; Jonkheijm, Pascal ; Brunsveld, Luc. / Directed Supramolecular Surface Assembly of SNAP-tag Fusion Proteins. In: Chemistry: a European journal. 2012 ; Vol. 18, No. 22. pp. 6788-6794.
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title = "Directed Supramolecular Surface Assembly of SNAP-tag Fusion Proteins",
abstract = "Supramolecular assembly of proteins on surfaces and vesicles was investigated by site-selective incorporation of a supramolecular guest element on proteins. Fluorescent proteins were site-selectively labeled with bisadamantane by SNAP-tag technology. The assembly of the bisadamantane functionalized SNAP-fusion proteins on cyclodextrin-coated surfaces yielded stable monolayers. The binding of the fusion proteins is specific and occurs with an affinity in the order of 106 M−1 as determined by surface plasmon resonance. Reversible micropatterns of the fusion proteins on micropatterned cyclodextrin surfaces were visualized by using fluorescence microscopy. Furthermore, the guest-functionalized proteins could be assembled out of solution specifically onto the surface of cyclodextrin vesicles. The SNAP-tag labeling of proteins thus allows for assembly of modified proteins through a host–guest interaction on different surfaces. This provides a new strategy in fabricating protein patterns on surfaces and takes advantage of the high labeling efficiency of the SNAP-tag with designed supramolecular elements",
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author = "D.A. Uhlenheuer and D. Wasserberg and C. Haase and Nguyen, {Hoang D.} and J.H. Schenkel and Jurriaan Huskens and B.J. Ravoo and Pascal Jonkheijm and Luc Brunsveld",
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Uhlenheuer, DA, Wasserberg, D, Haase, C, Nguyen, HD, Schenkel, JH, Huskens, J, Ravoo, BJ, Jonkheijm, P & Brunsveld, L 2012, 'Directed Supramolecular Surface Assembly of SNAP-tag Fusion Proteins', Chemistry: a European journal, vol. 18, no. 22, pp. 6788-6794. https://doi.org/10.1002/chem.201200238

Directed Supramolecular Surface Assembly of SNAP-tag Fusion Proteins. / Uhlenheuer, D.A.; Wasserberg, D.; Haase, C.; Nguyen, Hoang D.; Schenkel, J.H.; Huskens, Jurriaan; Ravoo, B.J.; Jonkheijm, Pascal; Brunsveld, Luc.

In: Chemistry: a European journal, Vol. 18, No. 22, 2012, p. 6788-6794.

Research output: Contribution to journalArticleAcademicpeer-review

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T1 - Directed Supramolecular Surface Assembly of SNAP-tag Fusion Proteins

AU - Uhlenheuer, D.A.

AU - Wasserberg, D.

AU - Haase, C.

AU - Nguyen, Hoang D.

AU - Schenkel, J.H.

AU - Huskens, Jurriaan

AU - Ravoo, B.J.

AU - Jonkheijm, Pascal

AU - Brunsveld, Luc

PY - 2012

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N2 - Supramolecular assembly of proteins on surfaces and vesicles was investigated by site-selective incorporation of a supramolecular guest element on proteins. Fluorescent proteins were site-selectively labeled with bisadamantane by SNAP-tag technology. The assembly of the bisadamantane functionalized SNAP-fusion proteins on cyclodextrin-coated surfaces yielded stable monolayers. The binding of the fusion proteins is specific and occurs with an affinity in the order of 106 M−1 as determined by surface plasmon resonance. Reversible micropatterns of the fusion proteins on micropatterned cyclodextrin surfaces were visualized by using fluorescence microscopy. Furthermore, the guest-functionalized proteins could be assembled out of solution specifically onto the surface of cyclodextrin vesicles. The SNAP-tag labeling of proteins thus allows for assembly of modified proteins through a host–guest interaction on different surfaces. This provides a new strategy in fabricating protein patterns on surfaces and takes advantage of the high labeling efficiency of the SNAP-tag with designed supramolecular elements

AB - Supramolecular assembly of proteins on surfaces and vesicles was investigated by site-selective incorporation of a supramolecular guest element on proteins. Fluorescent proteins were site-selectively labeled with bisadamantane by SNAP-tag technology. The assembly of the bisadamantane functionalized SNAP-fusion proteins on cyclodextrin-coated surfaces yielded stable monolayers. The binding of the fusion proteins is specific and occurs with an affinity in the order of 106 M−1 as determined by surface plasmon resonance. Reversible micropatterns of the fusion proteins on micropatterned cyclodextrin surfaces were visualized by using fluorescence microscopy. Furthermore, the guest-functionalized proteins could be assembled out of solution specifically onto the surface of cyclodextrin vesicles. The SNAP-tag labeling of proteins thus allows for assembly of modified proteins through a host–guest interaction on different surfaces. This provides a new strategy in fabricating protein patterns on surfaces and takes advantage of the high labeling efficiency of the SNAP-tag with designed supramolecular elements

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