Both authors contributed equally.
Control of Nanomolar Interaction and In Situ Assembly of Proteins in Four Dimensions by Light†
Article first published online: 2 JAN 2013
Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 52, Issue 3, pages 848–853, January 14, 2013
How to Cite
Labòria, N., Wieneke, R. and Tampé, R. (2013), Control of Nanomolar Interaction and In Situ Assembly of Proteins in Four Dimensions by Light . Angew. Chem. Int. Ed., 52: 848–853. doi: 10.1002/anie.201206698
This work was supported by the DFG through Ta157/9 (SPP 1623), SFB 902 (B7), as well as ERA-Net-Neuron.
- Issue published online: 11 JAN 2013
- Article first published online: 2 JAN 2013
- Manuscript Revised: 10 OCT 2012
- Manuscript Received: 18 AUG 2012
- 3D photopatterning;
- caged compounds;
- molecular recognition;
- protein assembly
Making light work: Photoactivatable multivalent trisNTA compounds have been developed for the in situ labeling and assembly of His-tagged proteins in time and space (see picture). This small light-tunable lock-and-key system offers the opportunity to trigger nanomolar protein interactions, such as receptor clustering, or biotechnological applications, for example, multiprotein arrays.