Size‐Controlled Ni Nanocrystal Growth on Peptide Nanotubes and Their Magnetic Properties

Abstract

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Mechanical‐Force‐Induced Nucleation and Growth of Peptide Nanofibers at Liquid/Solid Interfaces

“…[1] In this category are ionic-complementary peptides, which contain a repeating charge distribution and alternating hydrophobic and hydrophilic residues in the amino acid sequence; this leads to an unusual combination of amphiphilicity and chemical complementarity. Such peptides can self-assemble into stable nanostructures through electrostatic interactions, hydrogen bonds, and hydrophobic interactions.[1a, 2] Their nanostructures have a large number of potential applications, such as templates for nanofabrication, [3] scaffoldings for tissue repair and engineering, [4] nanocarriers for drug and gene/ small interfering RNA delivery, [5] and surface modifiers for enzyme immobilization in biosensors. [6] Many of these processes involve interface and surface patterning with peptide micro-/nanostructures.…”

One‐Dimensional Magnetic Nanowires Obtained by Protein Fibril Biotemplating

“…Although biotemplating of metallic nanowires by peptides and protein fibrils has been reported previously, [8a, 18] less attention has been paid to the production of 1D protein fibril-templated magnetic structures, and their magnetic properties have not been analysed in detail. Bolaamphiphile peptide fibrils, for example, have been used to template the growth and size of nickel nanocrystals on their surfaces and to tune their magnetic properties, [19] self-assembled peptides have also been conjugated to gadolinium ions, [20] and iron bionanomineralisation has been found to occur in human serum transferrin fibrils. [21] Results and Discussion Nanowire synthesis and characterisation: For in situ magnetic nanoparticle formation and subsequent fibril coverage, nanoparticle-coated protein fibrils were obtained by sequential addition of Fe 2 + and Fe 3 + ions (1:2 molar ratio) and ammonium hydroxide (NH 4 OH) solutions to aqueous solutions containing self-assembled fibrils, with subsequent incubation at 80 8C (see the Experimental Section for protein fibrillation and nanoparticle growth details).…”

Metallic nanowires on a new protein template

“…The bio-templated self-assembly of these nanowires, takes advantage of the nanoscale dimensions of various peptides, proteins and DNA. Some peptides have the capacity to self-assemble into 1-D structures and to subsequently serve as templates for various conducting or semiconducting nanowires [5][6][7][8]. Other structures that have been used as biotemplates include microtubules [9][10][11], β-amyloid [7,12], the yeast prion protein Sup35NM [13], and the tobacco mosaic virus [14].…”