Anchoring of liquid crystals on biomolecular interfaces

The research described in this thesis advances our understanding of the intermolecular interactions that drive the ordering of nematic liquid crystals at biomolecular interfaces. While many prior studies have investigated the ordering of liquid crystals on surfaces decorated with biomolecules such as oligopeptides, proteins, DNA, viruses and others, the complexity of the biomolecules used in these studies have largely prevented the systematic study of the interactions that dominate the ordering of the LCs. We propose that studies of the intermolecular interactions of LCs with simpler biomolecules (i.e. dipeptides and oligopeptides) will permit the elucidation of the mechanisms of interaction that influence LC ordering on biomolecular interfaces.;The first section of this thesis describes the characterization of the covalent attachment and orientation of a biologically-relevant oligopeptide using near edge x-ray absorption fine structure spectroscopy (NEXAFS). We note that relatively few methods exist to characterize biomolecules at monolayer and sub-monolayer coverages on surfaces, and that characterization of the structure and organization of biomolecules on surfaces is especially challenging.;The second section of this thesis includes several studies of the orientational ordering of LCs supporting on organized monolayers of dipeptides, with the goal of understanding how peptide-based interfaces encode intermolecular interactions that are amplified into supramolecular ordering. We demonstrate that long-range order present in dipeptide monolayers define patterns of intermolecular interactions (e.g. hydrogen bonds) that influence the ordering of LCs. These studies provide novel insights into the organization of surface-immobilized dipeptides and elucidate how chemical transformations and chirality of biomolecules can be transduced into orientational ordering of LCs.;The final section of this thesis suggests an area of future research and provides preliminary results regarding the use of LC ordering to report the phosphorylation of an oligopeptide that is a peptide substrate of the epidermal growth factor receptor (EGFR).;The research in this thesis, when combined, advances the understanding of the organization of surface-immobilized biomolecules and their influence on the orientational ordering of LCs.