Orientations of nematic liquid crystals on surfaces presenting controlled densities of peptides: amplification of protein-peptide binding events.
We report a study of the orientations of nematic liquid crystals (LCs) in contact with peptide-modified, oligoethylene glycol-containing, self-assembled monolayers (SAMs). The SAMs were formed on gold films that were prepared by physical vapor deposition at an oblique angle of incidence. Two peptides were investigated: the optimized substrate for the Src protein kinase (IYGEFKKKC) and the synthetic equivalent of that peptide after kinase modification (IpYGEFKKKC). Polarization modulation-infrared reflectance absorbance spectroscopy (PM-IRRAS) was used to characterize the relative areal densities and orientations of these peptides at the interface. We conclude that the presence/absence of a phosphate group can influence the maximum packing density of immobilized peptide. We evaluated the orientations of the nematic liquid crystal 5CB in contact with these peptide-modified surfaces by using polarized microscopy. The time required for the nematic phase of 5CB to exhibit long-range orientational ordering (uniform alignment) was found to increase with increasing areal densities of immobilized peptide. We also found that the specific binding event between anti-phosphotyrosine IgG and the surface-immobilized phosphopeptide leads to an increase in the time required for the liquid crystal to achieve uniform anchoring (exceeding the experimentally accessible time scales). These results, when combined, suggest that the areal density and size of biomolecules at an interface can influence the time required for liquid crystals in contact with nanostructured surfaces to exhibit long-range orientational order. Finally, we illustrate the potential utility of this system by demonstrating that liquid crystals can be used to amplify and report protein binding events occurring on a spatially resolved peptide array.
Clare
Brian H
BH
Department of Chemical and Biological Engineering, University of Wisconsin-Madison, 1415 Engineering Drive, Madison, Wisconsin 53706, USA.
Abbott
Nicholas L
NL
D000595:Amino Acid Sequence; D003460:Crystallization; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D017550:Spectroscopy, Fourier Transform Infrared; D013499:Surface Properties
D010455:Peptides; D011506:Proteins