In situ assembly of macromolecular complexes triggered by light

Autor(en): Grunwald, Christian
Schulze, Katrin
Reichel, Annett
Weiss, Victor U.
Blaas, Dieter
Piehler, Jacob 
Wiesmueller, Karl-Heinz
Tampe, Robert
Stichwörter: biofunctionalized interface; FLUORESCENT; IMMOBILIZATION; light-triggerd chemical biology; molecular recognition; Multidisciplinary Sciences; PROBES; protein interaction; PROTEINS; Science & Technology - Other Topics; self-assembly by light; SURFACES
Erscheinungsdatum: 2010
Herausgeber: NATL ACAD SCIENCES
Journal: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volumen: 107
Ausgabe: 14
Startseite: 6146
Seitenende: 6151
Zusammenfassung: 
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.
ISSN: 00278424
DOI: 10.1073/pnas.0912617107

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