This work reports research on the development of bimodal magnetic and fluorescent 1D nanoprobes. First, ferromagnetic nickel nanowires (NiNW) have been prepared by Ni electrodeposition in an anodic aluminum oxide (AAO) template. The highly ordered self-assembled AAO nanoporous templates were fabricated using a two-step anodization method of aluminum foil. The surface of the NiNW were then modified with polyethyleneimine (PEI) which was previously labeled with an organic dye (fluorescein isothiocyanate: FITC) via covalent bonding. The ensuing functionalized NiNW exhibited the characteristic green fluorescence of FITC and could be magnetically separated from aqueous solutions by using a NdFeB magnet. Finally, the interest of these bimodal NiNW as nanoprobes for in vitro cell separation and biolabeling was preliminary assessed in a proof of principle experiment that involved the attachment of bio-functionalized NiNW to blood cells. (C) 2013 Elsevier Inc. All rights reserved.

Aromatic peptides including diphenylalanine (FF) have the capacity to self-assemble into ordered, biocompatible nanostructures with piezoelectric properties relevant to a variety of biomedical applications. Electric fields are commonly applied to align FF nanotubes, yet little is known about the effect of the electric field on the assembly process. Using all-atom molecular dynamics with explicit water molecules, we examine the response of FF monomers to the application of a constant external electric field over a range of intensities. We probe the aggregation mechanism of FF peptides, and find that the presence of even relatively weak fields can accelerate ordered aggregation, primarily by facilitating the alignment of individual molecular dipole moments. This is modulated by the conformational response of individual FF peptides (e.g., backbone stretching) and by the cooperative alignment of neighboring FF and water molecules. These observations may facilitate future studies on the controlled formation of nanostructured aggregates of piezoelectric peptides and the understanding of their electro-mechanical properties. (C) 2014 Elsevier B.V. All rights reserved.