Diacetylene Chelator Lipids as Support for Immobilization and Imaging of Proteins by Atomic Force Microscopy
Abstract
Chelator lipids represent a powerful and flexible tool to immobilize, orient, and crystallize histidine-tagged proteins at interfaces. To produce stable two-dimensional polymers that are biofunctional, we synthesized diacetylene lipids carrying a metal-chelating headgroup. These lipids were characterized at the air−water interface with respect to their thermodynamic properties, complex formation, and photopolymerization using film balance techniques combined with epi-fluorescence microscopy. Polymerized monolayers were transferred onto solid supports and reversible binding of histidine-tagged protein/DNA complexes was followed by atomic force microscopy. The versatility of the chelator lipid concept may open the possibility to examine structure and function of proteins or multiprotein assemblies under native conditions and in real time by scanning probe microscopy.
Additional Information
© 1998 American Chemical Society. Received March 10, 1998. In Final Form: May 19, 1998. We thank Hermann Gaub, Walter Häckl, Hans Ribi, Jarl Rosenholm, Erich Sackmann, Lutz Schmitt, and Rudolf Simson for helpful discussions, as well as Wolfram Schäfer and Isolde Sonnenbichler for providing the MS and NMR spectra. We grateful acknowledge Oliver Boscheinen and Klaus-Dieter Scharf for supplying the HSF/DNA complex. This work was supported by the Deutsche Forschungsgemeinschaft and the European Commission (BIOTECH program).Additional details
- Eprint ID
- 88037
- DOI
- 10.1021/la980284p
- Resolver ID
- CaltechAUTHORS:20180719-160429047
- Deutsche Forschungsgemeinschaft (DFG)
- European Commission
- Created
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2018-07-19Created from EPrint's datestamp field
- Updated
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2021-11-16Created from EPrint's last_modified field