Liquid crystals anchored on mixed monolayers of chiral versus achiral molecules: continuous change in orientation as a function of enantiomeric excess.

The orientations of liquid crystals (LCs) anchored on monolayers formed from mixtures of chiral versus achiral molecules were compared. Changes in the enantiomeric excess of mixed monolayers of chiral dipeptides gave rise to continuous changes in the orientations of nematic LCs, allowing arbitrary tuning of the azimuthal orientations of LCs over a range of ≈100°. In contrast, the same LCs exhibited discontinuous changes in orientation on surfaces presenting mixtures of achiral molecules. These striking differences in the anchoring of LCs on surfaces presenting chiral versus achiral molecules provide insights into the molecular origins of ordering transitions of LCs, and provide new principles based on chiral monolayers for the rational design of surfaces that permit continuous tuning of the orientations of LCs.

Imide photodissociation investigated by X-ray absorption spectroscopy.

X-ray absorption spectroscopy is used to investigate the photodissociation of the imides PMDI (pyromellitic diimide) and SSMCC (sulfosuccinimidyl 4-(N-maleimidomethyl) cyclohexane-1-carboxylate). PMDI contains only one type of imide, and its photodissociation can be explained by a simple conversion from imide to a mix of imine and nitrile after desorption of the oxygens from the imide. SSMCC contains two different imides. One reacts like PMDI, the other in a more complex multistep process. Eventually, N(2) is formed in the bulk of the sample at high radiation density. The sequence of reactions is inferred from the π* peaks in total electron yield and fluorescence yield absorption spectra at the N 1s and O 1s edges. First-order rate equations are used to model the evolution of the peak areas versus radiation dose.

Enantiomeric interactions between liquid crystals and organized monolayers of tyrosine-containing dipeptides.

We have examined the orientational ordering of nematic liquid crystals (LCs) supported on organized monolayers of dipeptides with the goal of understanding how peptide-based interfaces encode intermolecular interactions that are amplified into supramolecular ordering. By characterizing the orientations of nematic LCs (4-cyano-4'-pentylbiphenyl and TL205 (a mixture of mesogens containing cyclohexane-fluorinated biphenyls and fluorinated terphenyls)) on monolayers of l-cysteine-l-tyrosine, l-cysteine-l-phenylalanine, or l-cysteine-l-phosphotyrosine formed on crystallographically textured films of gold, we conclude that patterns of hydrogen bonds generated by the organized monolayers of dipeptides are transduced via macroscopic orientational ordering of the LCs. This conclusion is supported by the observation that the ordering exhibited by the achiral LCs is specific to the enantiomers used to form the dipeptide-based monolayers. The dominant role of the -OH group of tyrosine in dictating the patterns of hydrogen bonds that orient the LCs was also evidenced by the effects of phosphorylation of the tyrosine on the ordering of the LCs. Overall, these results reveal that crystallographic texturing of gold films can direct the formation of monolayers of dipeptides with long-range order, thus unmasking the influence of hydrogen bonding, chirality, and phosphorylation on the macroscopic orientational ordering of LCs supported on these surfaces. These results suggest new approaches based on supramolecular assembly for reporting the chemical functionality and stereochemistry of synthetic and biological peptide-based molecules displayed at surfaces.

Universal mechanism for breaking amide bonds by ionizing radiation.

The photodissociation of the amide bond by UV light and soft x-rays is investigated by x-ray absorption spectroscopy at the C, N, and O 1s edges. Irradiation leaves a clear and universal signature for a wide variety of amides, ranging from oligopeptides to large proteins and synthetic polyamides, such as nylon. As the π∗ peak of the amide bond shrinks, two new π∗ peaks appear at the N 1s edge with a characteristic splitting of 1.1 eV. An additional characteristic is the overall intensity reduction of both the π∗ and σ∗ features at the O 1s edge, which indicates loss of oxygen. The spectroscopic results are consistent with the release of the O atom from the amide bond, followed by the migration of the H atom from the N to one of its two C neighbors. Migration to the carbonyl C leads to an imine, and migration to the C(α) of the amino acid residue leads to a nitrile. Imine and nitrile produce the two characteristic π∗ transitions at the N 1s edge. A variety of other models is considered and tested against the N 1s spectra of reference compounds.

Recent advances in colloidal and interfacial phenomena involving liquid crystals.

This feature article describes recent advances in several areas of research involving the interfacial ordering of liquid crystals (LCs). The first advance revolves around the ordering of LCs at bio/chemically functionalized surfaces. Whereas the majority of past studies of surface-induced ordering of LCs have involved surfaces of solids that present a limited diversity of chemical functional groups (surfaces at which van der Waals forces dominate surface-induced ordering), recent studies have moved to investigate the ordering of LCs on chemically complex surfaces. For example, surfaces decorated with biomolecules (e.g., oligopeptides and proteins) and transition-metal ions have been investigated, leading to an understanding of the roles that metal-ligand coordination interactions, electrical double layers, acid-base interactions, and hydrogen bonding can play in the interfacial ordering of LCs. The opportunity to create chemically responsive LCs capable of undergoing ordering transitions in the presence of targeted molecular events (e.g., ligand exchange around a metal center) has emerged from these fundamental studies. A second advance has focused on investigations of the ordering of LCs at interfaces with immiscible isotropic fluids, particularly water. In contrast to prior studies of surface-induced ordering of LCs on solid surfaces, LC-aqueous interfaces are deformable and molecules at these interfaces exhibit high levels of mobility and thus can reorganize in response to changes in the interfacial environment. A range of fundamental investigations involving these LC-aqueous interfaces have revealed that (i) the spatial and temporal characteristics of assemblies formed from biomolecular interactions can be reported by surface-driven ordering transitions in the LCs, (ii) the interfacial phase behavior of molecules and colloids can be coupled to (and manipulated via) the ordering (and nematic elasticity) of LCs, and (iii) the confinement of LCs leads to unanticipated size-dependent ordering (particularly in the context of LC emulsion droplets). The third and final advance addressed in this article involves interactions between colloids mediated by LCs. Recent experiments involving microparticles deposited at the LC-aqueous interface have revealed that LC-mediated interactions can drive interfacial assemblies of particles through reversible ordering transitions (e.g., from 1D chains to 2D arrays with local hexagonal symmetry). In addition, recent single-nanoparticle measurements suggest that the ordering of LCs about nanoparticles differs substantially from micrometer-sized particles and that the interactions between nanoparticles mediated by the LCs are far weaker than predicted by theory (sufficiently weak that the interactions are reversible and thus enable self-assembly). Finally, LC-mediated interactions between colloidal particles have also been shown to lead to the formation of colloid-in-LC gels that possess mechanical properties relevant to the design of materials that interface with living biological systems. Overall, these three topics serve to illustrate the broad opportunities that exist to do fundamental interfacial science and discovery-oriented research involving LCs.

Characterization of surfaces presenting covalently immobilized oligopeptides using near-edge X-ray absorption fine structure spectroscopy.

This study addresses the need for methods that validate the surface chemistry leading to the immobilization of biomolecules and provide information about the resulting structural configurations. We report on the use of near-edge X-ray absorption fine structure spectroscopy (NEXAFS) to characterize a widely employed immobilization chemistry that leads to the covalent attachment of a biologically relevant oligopeptide to a surface. The oligopeptide used in this study is a kinase substrate of the epidermal growth factor receptor (EGFR), a protein that is a common target for cancer therapeutics. By observing changes in the pi* and sigma* orbitals of specific nitrogen and carbon atoms (amide, imide, carbonyl), we are able to follow the sequential reactions leading to immobilization of the oligopeptide. We also show that it is possible to use NEXAFS to extend this characterization method to submonolayer densities that are relevant to biological assays. Such an element-specific chemical characterization of small peptides on surfaces fills an unmet need and establishes NEXAFS as useful technique for characterizing the immobilization of small biomolecules on surfaces.

Design of surfaces for liquid crystal-based bioanalytical assays.

Surface-induced ordering of liquid crystals (LCs) offers the basis of a label-free analytical technique for the detection of surface-bound biomolecules. The orientation-dependent energy of interaction of a LC with a surface (anchoring energy of LC), in particular, is both sensitive to the presence of surface-bound molecules and easily quantified. Herein, we report a study that analyzes a simple model of twisted nematic LC systems and thereby identifies surfaces with LC anchoring energies in the range of 0.5 microJ/m(2) to 2.0 microJ/m(2) to be optimal for use with LC-based analytical methods. Guided by these predictions, we demonstrate that analytic surfaces possessing anchoring energies within this range can be fabricated with a high level of precision (< 0.1 microJ/m(2)) through formation of monolayers of organothiols (with omega-functional groups corresponding to oligoethyleneglycols and amines) on gold films deposited by physical vapor deposition at oblique angles of incidence. Finally, by using the human epidermal growth factor receptor (EGFR) as a model protein analyte, we have characterized the influence of the anchoring energies of the surfaces on the response of the LC to the presence of surface-bound EGFR. These results, when combined with (32)P-radiolabeling of the EGFR to independently quantify the surface concentration of EGFR, permit identification of surfaces that allow use of LCs to report surface densities of EGFR of 30-40 pg/mm(2). Overall, the results reported in this paper guide the design of surfaces for use in LC-based analytical systems.