This work was supported in part by a Grant-in-Aid for Scientific Research on Priority Area (Grant No. 17 076 014), the High-Tech Research Center Program, the Center of Excellence (COE) Program for the 21st Century, and the Formation of Innovation Center for Fusion of Advanced Technologies in the Special Coordination Funds for Promoting Science and Technology, from the Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japan.
A Novel Approach to Observing Synergy Effects of PHSRN on Integrin–RGD Binding Using Intelligent Surfaces†
Article first published online: 19 JUN 2008
Copyright © 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Volume 20, Issue 16, pages 3034–3038, August 18, 2008
How to Cite
Ebara, M., Yamato, M., Aoyagi, T., Kikuchi, A., Sakai, K. and Okano, T. (2008), A Novel Approach to Observing Synergy Effects of PHSRN on Integrin–RGD Binding Using Intelligent Surfaces. Adv. Mater., 20: 3034–3038. doi: 10.1002/adma.200702308
- Issue published online: 14 AUG 2008
- Article first published online: 19 JUN 2008
- Manuscript Revised: 21 NOV 2007
- Manuscript Received: 11 SEP 2007
- stimuli-responsive polymers;
- surface modification;
- thermoresponsive materials
A novel assay for measuring time-dependant ligand-receptor affinity changes is developed based on a peptide-immobilized temperature-responsive surface, as schematically illustrated in the figure. The grafted thermoresponsive polymer acts as an “on-off” switch for mediating integrin–peptide bonding. At temperatures above and below the lower critical solution temperature (LCST), the peptides are accessible and shielded from integrin access, respectively.