Immobilization of ferrocene-modified SNAP-fusion proteins

D. Wasserberg, D. Uhlenheuer, P. Neirynck, Pauline Neirynck, Jordi Cabanas Danés, J.H. Schenkel, B.J. Ravoo, Q. An, Jurriaan Huskens, L.G. Milroy, Luc Brunsveld, Pascal Jonkheijm

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Abstract

The supramolecular assembly of proteins on surfaces has been investigated via the site-selective incorporation of a supramolecular moiety on proteins. To this end, fluorescent proteins have been site-selectively labeled with ferrocenes, as supramolecular guest moieties, via SNAP-tag technology. The assembly of guest-functionalized SNAP-fusion proteins on cyclodextrin- and cucurbit[7]uril-coated surfaces yielded stable monolayers. The binding of all ferrocene fusion proteins is specific as determined by surface plasmon resonance. Micropatterns of the fusion proteins, on patterned cyclodextrin and cucurbituril surfaces, have been visualized using fluorescence microscopy. The SNAP-fusion proteins were also immobilized on cyclodextrin vesicles. The supramolecular SNAP-tag labeling of proteins, thus, allows for the assembly of modified proteins via supramolecular host-guest interaction on different surfaces in a controlled manner. These findings extend the toolbox of fabricating supramolecular protein patterns on surfaces taking advantage of the high labeling efficiency of the SNAP-tag with versatile supramolecular moieties
Original languageEnglish
Pages (from-to)4066-4080
Number of pages15
JournalInternational journal of molecular sciences
Volume14
Issue number2
DOIs
Publication statusPublished - 2013

Fingerprint

SNAP
immobilization
Immobilization
Fusion reactions
fusion
proteins
Proteins
Cyclodextrins
assembly
Labeling
marking
ferrocene
ferrocenes
Surface Plasmon Resonance
Fluorescence microscopy
Fluorescence Microscopy
Surface plasmon resonance
surface plasmon resonance
Membrane Proteins
Monolayers

Keywords

  • METIS-301602
  • IR-90133

Cite this

Wasserberg, D., Uhlenheuer, D., Neirynck, P., Neirynck, P., Cabanas Danés, J., Schenkel, J. H., ... Jonkheijm, P. (2013). Immobilization of ferrocene-modified SNAP-fusion proteins. International journal of molecular sciences, 14(2), 4066-4080. https://doi.org/10.3390/ijms14024066
Wasserberg, D. ; Uhlenheuer, D. ; Neirynck, P. ; Neirynck, Pauline ; Cabanas Danés, Jordi ; Schenkel, J.H. ; Ravoo, B.J. ; An, Q. ; Huskens, Jurriaan ; Milroy, L.G. ; Brunsveld, Luc ; Jonkheijm, Pascal. / Immobilization of ferrocene-modified SNAP-fusion proteins. In: International journal of molecular sciences. 2013 ; Vol. 14, No. 2. pp. 4066-4080.
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abstract = "The supramolecular assembly of proteins on surfaces has been investigated via the site-selective incorporation of a supramolecular moiety on proteins. To this end, fluorescent proteins have been site-selectively labeled with ferrocenes, as supramolecular guest moieties, via SNAP-tag technology. The assembly of guest-functionalized SNAP-fusion proteins on cyclodextrin- and cucurbit[7]uril-coated surfaces yielded stable monolayers. The binding of all ferrocene fusion proteins is specific as determined by surface plasmon resonance. Micropatterns of the fusion proteins, on patterned cyclodextrin and cucurbituril surfaces, have been visualized using fluorescence microscopy. The SNAP-fusion proteins were also immobilized on cyclodextrin vesicles. The supramolecular SNAP-tag labeling of proteins, thus, allows for the assembly of modified proteins via supramolecular host-guest interaction on different surfaces in a controlled manner. These findings extend the toolbox of fabricating supramolecular protein patterns on surfaces taking advantage of the high labeling efficiency of the SNAP-tag with versatile supramolecular moieties",
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author = "D. Wasserberg and D. Uhlenheuer and P. Neirynck and Pauline Neirynck and {Cabanas Dan{\'e}s}, Jordi and J.H. Schenkel and B.J. Ravoo and Q. An and Jurriaan Huskens and L.G. Milroy and Luc Brunsveld and Pascal Jonkheijm",
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Wasserberg, D, Uhlenheuer, D, Neirynck, P, Neirynck, P, Cabanas Danés, J, Schenkel, JH, Ravoo, BJ, An, Q, Huskens, J, Milroy, LG, Brunsveld, L & Jonkheijm, P 2013, 'Immobilization of ferrocene-modified SNAP-fusion proteins' International journal of molecular sciences, vol. 14, no. 2, pp. 4066-4080. https://doi.org/10.3390/ijms14024066

Immobilization of ferrocene-modified SNAP-fusion proteins. / Wasserberg, D.; Uhlenheuer, D.; Neirynck, P.; Neirynck, Pauline; Cabanas Danés, Jordi; Schenkel, J.H.; Ravoo, B.J.; An, Q.; Huskens, Jurriaan; Milroy, L.G.; Brunsveld, Luc; Jonkheijm, Pascal.

In: International journal of molecular sciences, Vol. 14, No. 2, 2013, p. 4066-4080.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Immobilization of ferrocene-modified SNAP-fusion proteins

AU - Wasserberg, D.

AU - Uhlenheuer, D.

AU - Neirynck, P.

AU - Neirynck, Pauline

AU - Cabanas Danés, Jordi

AU - Schenkel, J.H.

AU - Ravoo, B.J.

AU - An, Q.

AU - Huskens, Jurriaan

AU - Milroy, L.G.

AU - Brunsveld, Luc

AU - Jonkheijm, Pascal

PY - 2013

Y1 - 2013

N2 - The supramolecular assembly of proteins on surfaces has been investigated via the site-selective incorporation of a supramolecular moiety on proteins. To this end, fluorescent proteins have been site-selectively labeled with ferrocenes, as supramolecular guest moieties, via SNAP-tag technology. The assembly of guest-functionalized SNAP-fusion proteins on cyclodextrin- and cucurbit[7]uril-coated surfaces yielded stable monolayers. The binding of all ferrocene fusion proteins is specific as determined by surface plasmon resonance. Micropatterns of the fusion proteins, on patterned cyclodextrin and cucurbituril surfaces, have been visualized using fluorescence microscopy. The SNAP-fusion proteins were also immobilized on cyclodextrin vesicles. The supramolecular SNAP-tag labeling of proteins, thus, allows for the assembly of modified proteins via supramolecular host-guest interaction on different surfaces in a controlled manner. These findings extend the toolbox of fabricating supramolecular protein patterns on surfaces taking advantage of the high labeling efficiency of the SNAP-tag with versatile supramolecular moieties

AB - The supramolecular assembly of proteins on surfaces has been investigated via the site-selective incorporation of a supramolecular moiety on proteins. To this end, fluorescent proteins have been site-selectively labeled with ferrocenes, as supramolecular guest moieties, via SNAP-tag technology. The assembly of guest-functionalized SNAP-fusion proteins on cyclodextrin- and cucurbit[7]uril-coated surfaces yielded stable monolayers. The binding of all ferrocene fusion proteins is specific as determined by surface plasmon resonance. Micropatterns of the fusion proteins, on patterned cyclodextrin and cucurbituril surfaces, have been visualized using fluorescence microscopy. The SNAP-fusion proteins were also immobilized on cyclodextrin vesicles. The supramolecular SNAP-tag labeling of proteins, thus, allows for the assembly of modified proteins via supramolecular host-guest interaction on different surfaces in a controlled manner. These findings extend the toolbox of fabricating supramolecular protein patterns on surfaces taking advantage of the high labeling efficiency of the SNAP-tag with versatile supramolecular moieties

KW - METIS-301602

KW - IR-90133

U2 - 10.3390/ijms14024066

DO - 10.3390/ijms14024066

M3 - Article

VL - 14

SP - 4066

EP - 4080

JO - International journal of molecular sciences

JF - International journal of molecular sciences

SN - 1661-6596

IS - 2

ER -

Wasserberg D, Uhlenheuer D, Neirynck P, Neirynck P, Cabanas Danés J, Schenkel JH et al. Immobilization of ferrocene-modified SNAP-fusion proteins. International journal of molecular sciences. 2013;14(2):4066-4080. https://doi.org/10.3390/ijms14024066