Liquid crystals (LCs) were used to amplify and transduce receptor-medi
ated binding of proteins at surfaces into optical outputs, Spontaneous
ly organized surfaces were designed so that protein molecules, upon bi
nding to ligands hosted on these surfaces, triggered changes in the or
ientations of 1- to 20-micrometer-thick films of supported LCs, thus c
orresponding to a reorientation of similar to 10(5) to 10(6) mesogens
per protein. Binding-induced changes in the intensity of light transmi
tted through the LC were easily seen with the naked eye and could be f
urther amplified by using surfaces designed so that protein-ligand rec
ognition causes twisted nematic LCs to untwist. This approach to the d
etection of ligand-receptor binding does not require labeling of the a
nalyte, does not require the use of electroanalytical apparatus, provi
des a spatial resolution of micrometers, and is sufficiently simple th
at it may find use in biochemical assays and imaging of spatially reso
lved chemical libraries.