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UW-Madison

  Abbott Research Group - UW Chemical and Biological Engineering

Laboratory for Molecular Engineering
Department of Chemical and Biological Engineering

Ordering of Liquid Crystals on Bio/Chemically Functionalized Interfaces


Revealed that the ordering of liquid crystals can be used to report the presence and state of biomolecules arrayed on the surfaces of solids (Science, 1998). Proteins captured onto designed surfaces were shown to lead to ordering behaviors of liquid crystals that permitted optical reporting of the proteins with a dynamic range that extended over four orders of magnitude in concentration (JACS, 2007). The use of liquid crystals to image patterned surfaces on the ~10µm scale was demonstrated. These studies are also revealing that the ordering of liquid crystals can be sensitive to (i) the orientations of proteins at surfaces (JACS, 2004) and (ii) post-translational changes in the states of proteins and peptides such as phosphorylation.

(Top) (A) Molecular structures of EGFR peptide Y1173. (B) Schematic illustration of a gold film supported on a glass slide on which a mixed monolayer of EG4 and EG4N is formed. The surface was activated using SSMCC to immobilize either Y1173 or pY1173. The figure shows an antibody binding to the immobilized peptide. (Bottom) Quantification of the anchoring energy of LC in contact with pY1173-modified self-assembled monolayers following incubation of the monolayers with phosphospecific antibody (filled data points). The right axis of the plot shows the deviation of the director Φ as a function of increasing concentration of the phosphospecific antibody (open data points). The concentration of EG4N in the solution used to form the mixed monolayers of EG4 and EG4N to which the peptides were covalently attached was 0.01μM.

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Molecular structures of EGFR peptide Y1173 filled data points