Photoactivatable caged cyclic RGD peptide for triggering integrin binding and cell adhesion to surfaces

Chembiochem. 2011 Nov 25;12(17):2623-9. doi: 10.1002/cbic.201100437. Epub 2011 Nov 4.

Abstract

We report the synthesis and properties of a photoactivatable caged RGD peptide and its application for phototriggering integrin- and cell-binding to surfaces. We analysed in detail 1) the differences in the integrin-binding affinity of the caged and uncaged forms by quartz crystal microbalance (QCM) studies, 2) the efficiency and yield of the photolytic uncaging reaction, 3) the biocompatibility of the photolysis by-products and irradiation conditions, 4) the possibility of site, temporal and density control of integrin-binding and therefore human cell attachment, and 5) the possibility of in situ generation of cell patterns and cell gradients by controlling the UV exposure. These studies provide a clear picture of the potential and limitations of caged RGD for integrin-mediated cell adhesion and demonstrate the application of this approach to the control and study of cell interactions and responses.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Adhesion
  • Cells, Cultured
  • Humans
  • Integrins / metabolism*
  • Peptides, Cyclic / metabolism*
  • Protein Binding
  • Quartz Crystal Microbalance Techniques
  • Ultraviolet Rays

Substances

  • Integrins
  • Peptides, Cyclic
  • cyclic arginine-glycine-aspartic acid peptide