Nanomechanical force measurements of gliadin protein interactions

The strength and nature of interactions between monomeric gliadin proteins involving alpha-alpha, omega-omega, and alpha-omega interactions in 0.01M acetic acid, and the effect of urea has been investigated. It was shown by means of nanomechanical force measurements that the stretching events in the separation curve after adhesive phenomena originated from proteins. These stretching events displayed different responses of the alpha- and omega-gliadins to urea. While 2M urea caused the more globular alpha-gliadins to unfold, the beta-turn-rich omega-gliadins remained fairly stable even in 8M urea. This suggests different roles for gliadins in the formation of dough; while the omega-gliadins are still in a compact structure being responsible for the viscous flow, the alpha-gliadins have already started to participate in forming the network in dough.     

Influence of Substrate on Plasmon-Induced Absorption Enhancements

A set of periodic plasmonic nanostructures is designed and fabricated as a means to investigate light absorption in single-crystal silicon thin-film structures with silicon-on-insulator (SOI) wafers as a model system. It is shown both computationally and experimentally that plasmon-induced absorption enhancement is remarkably higher for such devices than for thick or semi-infinite structures or for the thin-film amorphous silicon solar cells reported in the literature. Experimental photocurrent enhancements of the orders of 12 and 20 are demonstrated for non-optimized 2200-nm-thick photoconductive and 300-nm-thick photovoltaic test structures, respectively. Theoretical absorption enhancements as high as 80 are predicted to be achievable for the similar structures. The features of the spectral enhancements observed are attributed to several interacting resonance phenomena: not just to the favourable scattering of light by the periodic plasmonic nanoparticle arrays into the SOI device layer and coupling to the waveguide modes interacting with the plasmonic array but also to the Fabry-Pérot type interferences in the layered structure. We show that the latter effect gives a significant contribution to the spectral features of the enhancements, although frequently ignored in the discussions of previous reports.

     

Lipoate-based imprinted self-assembled molecular thin films for biosensor applications

Lipoate derivatives were used for the formation of imprinted self-assembled molecular thin films for the recognition of morphine. A large collection of lipoate derivatives was screened by molecular dynamics simulations in various solvents. A set of ligands showing favourable interactions with morphine in aqueous environment was selected for synthesis. Morphine-imprinted layers were then produced on gold substrates in mixed monolayers with morphine added as the template. The binding of ligands and morphine to gold, as well as the association/dissociation of morphine to the formed layers were studied with Surface Plasmon Resonance. Imprinted factors were highly variable and were dependent on ligand/morphine mixing ratio, lipoate derivative and monolayer preparation method. The imprinted factors were as high as 100 and 600 for one of the ligands. The results show that the simulations are able to provide correct information of the relative strengths of the molecular interactions between the ligand and morphine molecules in different solutions. The liquid phase simulations are, however, not able to predict the imprinted factors (i.e. distinguish between specific and non-specific binding), because the specificity is not formed before self-assembly on the surface.     

Influence of rotational energy barriers to the conformational search of protein loops in molecular dynamics and ranking the conformations.

An adjustable-barrier dihedral angle potential was added as an extension to a novel, previously presented soft-core potential to study its contribution to the efficacy of the search of the conformational space in molecular dynamics. As opposed to the conventional soft-core potential functions, the leading principle in the design of the new soft-core potential, as well as of its extension, the soft-core and adjustable-barrier dihedral angle (SCADA) potential (referred as the SCADA potential), was to maintain the main equilibrium properties of the original force field. This qualifies the methods for a variety of a priori modeling problems without need for additional restraints typically required with the conventional soft-core potentials. In the present study, the different potential energy functions are applied to the problem of predicting loop conformations in proteins. Comparison of the performance of the soft-core and SCADA potential showed that the main hurdles for the efficient sampling of the conformational space of (loops in) proteins are related to the high-energy barriers caused by the Lennard-Jones and Coulombic energy terms, and not to the rotational barriers, although the conformational search can be further enhanced by lowering the rotational barriers of the dihedral angles. Finally, different evaluation methods were studied and a few promising criteria found to distinguish the near-native loop conformations from the wrong ones.