期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 107, 期 14, 页码 6146-6151出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0912617107
关键词
biofunctionalized interface; light-triggerd chemical biology; molecular recognition; protein interaction; self-assembly by light
资金
- Bundesministerium fur Bildung und Forschung [0312031, 0312034]
- Deutsche Forschungsgemeinschaft [Ta157/6]
- Austrian Science Foundation (FWF)
Chemical biology aims for a perfect control of protein complexes in time and space by their site-specific labeling, manipulation, and structured organization. Here we developed a self-inactivated, lock-and-key recognition element whose binding to His-tagged proteins can be triggered by light from zero to nanomolar affinity. Activation is achieved by photocleavage of a tethered intramolecular ligand arming a multivalent chelator head for high-affinity protein interaction. We demonstrate site-specific, stable, and reversible binding in solution as well as at interfaces controlled by light with high temporal and spatial resolution. Multiplexed organization of protein complexes is realized by an iterative in situ writing and binding process via laser scanning microscopy. This light-triggered molecular recognition should allow for a spatiotemporal control of protein-protein interactions and cellular processes by light-triggered protein clustering.
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