Biomolecular Interactions at Phospholipid-Decorated Surfaces of Liquid Crystals
Jeffrey M. Brake,
Maren K. Daschner,
Yan-Yeung Luk,
Nicholas L. Abbott*
The spontaneous assembly of phospholipids at planar interfaces
between thermotropic liquid crystals and aqueous phases gives
rise to patterned orientations of the liquid crystals that reflect
the spatial and temporal organization of the phospholipids.
Strong and weak specific-binding events involving proteins at
these interfaces drive the reorganization of the phospholipids
and trigger orientational transitions in the liquid crystals.
Because these interfaces are fluid, processes involving the
lateral organization of proteins (such as the formation of protein-
and phospholipid-rich domains) are also readily imaged by the
orientational response of the liquid crystal, as are stereospecific
enzymatic events. These results provide principles for label-free
monitoring of aqueous streams for molecular and biomolecular
species without the need for complex instrumentation.
* To whom correspondence should be addressed. E-mail: abbott{at}engr.wisc.edu
