Next Article in Journal
Stabilized Conversion Efficiency and Dye-Sensitized Solar Cells from Beta vulgaris Pigment
Next Article in Special Issue
Molecular Self-Assembly at Metal-Electrolyte Interfaces
Previous Article in Journal
The Role of Lipid Domains in Bacterial Cell Processes
Previous Article in Special Issue
Self-Assembly of Pyridine-Modified Lipoic Acid Derivatives on Gold and Their Interaction with Thyroxine (T4)
Int. J. Mol. Sci. 2013, 14(2), 4066-4080; doi:10.3390/ijms14024066

Immobilization of Ferrocene-Modified SNAP-Fusion Proteins

, 2
, 2
, 1, 3
, 3
, 1
, 1
, 2
, 2 and 1,*
Received: 30 November 2012 / Revised: 4 February 2013 / Accepted: 4 February 2013 / Published: 18 February 2013
(This article belongs to the Special Issue Molecular Self-Assembly 2012)
View Full-Text   |   Download PDF [606 KB, uploaded 19 June 2014]   |   Browse Figures
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.
Keywords: host-guest chemistry; protein immobilization; protein modifications; cyclodextrin; cucurbituril; ferrocene host-guest chemistry; protein immobilization; protein modifications; cyclodextrin; cucurbituril; ferrocene
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Export to BibTeX |

MDPI and ACS Style

Wasserberg, D.; Uhlenheuer, D.A.; Neirynck, P.; Cabanas-Danés, J.; Schenkel, J.H.; Ravoo, B.J.; An, Q.; Huskens, J.; Milroy, L.-G.; Brunsveld, L.; Jonkheijm, P. Immobilization of Ferrocene-Modified SNAP-Fusion Proteins. Int. J. Mol. Sci. 2013, 14, 4066-4080.

AMA Style

Wasserberg D, Uhlenheuer DA, Neirynck P, Cabanas-Danés J, Schenkel JH, Ravoo BJ, An Q, Huskens J, Milroy L-G, Brunsveld L, Jonkheijm P. Immobilization of Ferrocene-Modified SNAP-Fusion Proteins. International Journal of Molecular Sciences. 2013; 14(2):4066-4080.

Chicago/Turabian Style

Wasserberg, Dorothee; Uhlenheuer, Dana A.; Neirynck, Pauline; Cabanas-Danés, Jordi; Schenkel, Jan H.; Ravoo, Bart J.; An, Qi; Huskens, Jurriaan; Milroy, Lech-Gustav; Brunsveld, Luc; Jonkheijm, Pascal. 2013. "Immobilization of Ferrocene-Modified SNAP-Fusion Proteins." Int. J. Mol. Sci. 14, no. 2: 4066-4080.

Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert