Protein-templated semiconductor nanoparticle chains

Abstract

Cadmium sulfide and lead sulfide semiconducting nanoparticle chains have been fabricated for the first time by exploiting a general property of proteins, amyloidogenicity. The diameter of the CdS and PbS nanowires was tuned in the range of ∼50 to ∼350 nm by changing the process parameters. The nanoparticle chains were characterized by field emission scanning electron microscopy, UV-visible spectroscopy, transmission electron microscopy, electron energy loss spectroscopy and high-resolution transmission electron microscopy.

Fabrication of ZnS nanoparticle chains on a protein template

“…However, peptides and proteins, with the ability to self-assemble into ordered fibrils have been much less investigated. While several metallic nanowires, as well as CdS nanoparticle chains have been synthesized via protein-directed nucleation and growth in our laboratory (Padalkar et al 2007, 2008), to our knowledge, there are no reports in literature regarding the use of fibrillar proteins for the template synthesis of zinc sulfide (ZnS) nanowires or nanoparticle chains. ZnS is an II–VI semiconducting material having a band gap of 3.7 eV.…”

Self-assembly and alignment of semiconductor nanoparticles on cellulose nanocrystals

“…The fabrication of nanoparticles onto the surface of a biological template, often, use electroless deposition techniques on account of the simplicity of the procedure and mild reaction conditions [30]. The driving force for nanoparticles deposition relies on the difference between the redox potentials of the precursor salt to those of the biomolecule template structure.…”

“…There are some reports in the literature on the use of CNCs as templates for the growth of electrically (semi) conducting polymers [28][29][30].…”

Palladium nanoparticles supported by amyloid fibrils: From size controllable synthesis to extremely high catalytic performance

“…However, the size and uniformity of Pd NPs coated on TMV1cys still cannot be well controlled, and it is also complicated to genetically engineer TMV to carry thiol groups on the exposed surface. Notably, amyloid fibrils provide another green alternative as scaffolds for nanostructure assembly [23][24][25][26][27][28]; their internal structures comprise a cross-␤ sheet core with rich hydrogen bonds formed between the amino and carbonyl groups of the polypeptide chain, thus making them remarkably stable even in harsh conditions [29]. Importantly, amyloid fibrils are rich in functional groups that can specifically interact with desired nanoparticles.…”