Self-Assembled Peptide Nanofiber Templated One-Dimensional Gold Nanostructures Exhibiting Resistive Switching

Abstract

An amyloid-like peptide molecule self-assembling into one-dimensional nanofiber structure in ethanol was designed and synthesized with functional groups that can bind to gold ions. The peptide nanofibers were used as templates for nucleation and growth of one-dimensional gold nanostructures in the presence of ascorbic acid as reducing agent. We performed multistep seed-mediated synthesis of gold nanoparticles by changing peptide/gold precursor and peptide/ reducing agent ratios. Gold nanostructures with a wide range of morphologies such as smooth nanowires, noodle-like onedimensional nanostructures, and uniform aggregates of spherical nanoparticles were synthesized by use of an environmentally friendly synthesis method. Nanoscale electrical properties of gold-peptide nanofibers were investigated using atomic force microscopy. Bias dependent current (IV) measurements on thin films of gold-peptide nanofiber hybrid revealed tunneling dominated transport and resistive switching. Gold-peptide nanofiber composite nanostructures can provide insight into electrical conduction in biomolecular/inorganic composites, highlighting their potential applications in electronics and optics.

Critical attributes of nanofibers: Preparation, drug loading, and tissue regeneration

“…Nanofibers can be produced using various techniques such as drawing (Ondarçuhu and Joachim, 1998), electrospinning, forcespinning (Sebe et al, 2013), interfacial polymerization (Zhang et al, 2004), melt blowing (Ellison et al, 2007), phase separation (Ma and Zhang, 1999), self-assembly (Acar et al, 2012), template melt extrusion (Li et al, 2006a), and template synthesis (Feng et al, 2002), as briefly presented in Table 2. Among the various known techniques for nanofiber production, electrospinning is the most frequently used due to its simplicity.…”

On the mechanism of protein-templated gold nanoparticle synthesis: Protein organization, controlled gold sequestration, and unexpected reaction products.

“…36 The development of new protein-based materials, however, has traditionally been left to using simple hydrophobic-hydrophilic interactions to drive their formation. [37][38][39] This has left a gap in our ability to mimic Nature, which uses proteins to drive the formation of nano-scale and macro-scale material architecture. While researchers have become proficient at designing materials with intricate geometry using DNA origami, [40][41][42][43] the ability to design and generate materials with proteins remains elusive.…”

From fibrous elastin proteins to one-dimensional transition metal phosphides and their applications

“…20,21 In these reports, the challenge remains to control the size and morphologies of the nanomaterials due to the effects of pH, ionic strength and temperature on the stability of these biological materials. 22,23 In addition, most biological materials are insoluble in organic solvents, further limiting their use in nanoscale metal sulde or phosphide synthesis via oil-phase methods. Hence, the search for suitable biological materials that allow TMP nanomaterial synthesis in both aqueous and organic phases is desired.…”