RESUMEN
A novel electrical bistable hybrid nanocomposite based on doped Polyaniline nanofibers with 1-Dodecanethiol-protected Gold nanoparticle (PAni.AuDT), 3-4 nm in size, as the conductive component and polystyrene as polymer matrix was prepared. The structural morphology of the composite and the dispersion of nanoparticles inside it were evaluated using Transmission Electron Microscopy (TEM). The thermal stability and the ratio Polyaniline/Gold nanoparticles in the composite were determined by using thermogravimetric analysis. The electrical bistability of the PAni.AuDT-PS composite, the influence of the dispersion of the PAni.AuDT conductive network and the basic operation mechanism, have been assessed by measuring the electrical response of planar device architectures, also as a function of the environmental temperature (in the range 200 K < T < 360 K). The basic operation mechanism of the hybrid compound has been then correlated to the combined action of the thermally-induced scattering of charge carriers and the thermal contraction of the hosting polymeric matrix. Moreover, the right compromise between these two effects in terms of the most efficient bistability has been studied, founding the concentration of the conductive component which optimizes the device on-off ratio (I(on)/ I(off)).
RESUMEN
There is a growing interest in identifying biomacromolecules such as proteins and peptides to functionalize metallic surfaces through noncovalent binding. One method for functionalizing materials without fundamentally changing their inherent structure is using biorecognition moieties. Here, we proved a general route to select a biomolecule adhesive motif for surface functionalization by comprehensively screening phage displayed peptides. In particular, we selected a genetically engineered M13 bacteriophage and a linear dodecapeptide derived from its pIII domain for recognizing gold surfaces in a specific and selective manner. In the phage context, we demonstrated the adhesive motif was capable to adsorb on gold in a preferential way with a morphological and viscoelastic signature of the adsorbed layer as evidenced by QCM-D and AFM investigations. Out of the phage context, the linear dodecapeptide is reproducibly found to adhere to the gold surface, and by quantitative SPR measurements, high affinity constants (K(eq)~10(6)M(-1), binding energy ~-8 kcal/mol) were determined. We proved that the interactions occurring at gold interface were mainly hydrophobic as a consequence of high frequency of hydrophobic residues in the peptide sequence. Moreover, by CD, molecular dynamics and steered molecular dynamics, we demonstrated that the molecular flexibility only played a minor role in the peptide adsorption. Such noncovalent but specific modification of inorganic surfaces through high affinity biomolecule adsorption represents a general strategy to modulate the functionality of multipurpose metallic surfaces.