When the surface is exposed to a solution containing many different proteins, only those with high affinities for the tethered small molecule selectively attach to the surface. The bound protein molecules can then be identified in place or removed for characterization. "The tethered neurotransmitter acts like a fishing pole," says Andrews. "When the small molecule 'bait' is correctly placed on the surface, it captures much larger molecules that interact with it in a biologically specific way."
As a result of this inherent selectivity, it is possible to identify biomolecules, by function, from a sea of thousands of different types of molecules. Weiss adds, "The key to obtaining a highly specific association is producing optimal spacing of the tethered neurotransmitters. The ideal spacing allows large molecules to recognize the functional groups of the small molecule while avoiding nonspecific binding to the surface itself."
Because of their selectivity, these materials are suitable for a variety of investigations in biological systems. "Each neurotransmitter can bind to a number of different receptors in the brain," says Andrews. "Some of these receptors are known, but there are many more to identify. Also, the numbers of receptors are altered in different disease states and in response to treatment, and these capture surfaces could be used to study how groups of functionally related proteins change in a coordinated fashion."
|Contact: Barbara K. Kennedy|