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1.
Adv Mater ; 31(18): e1900251, 2019 May.
Article in English | MEDLINE | ID: mdl-30907483

ABSTRACT

Unlike conventional plasmonic media, polaritonic van der Waals (vdW) materials hold promise for active control of light-matter interactions. The dispersion relations of elementary excitations such as phonons and plasmons can be tuned in layered vdW systems via stacking using functional substrates. In this work, infrared nanoimaging and nanospectroscopy of hyperbolic phonon polaritons are demonstrated in a novel vdW heterostructure combining hexagonal boron nitride (hBN) and vanadium dioxide (VO2 ). It is observed that the insulator-to-metal transition in VO2 has a profound impact on the polaritons in the proximal hBN layer. In effect, the real-space propagation of hyperbolic polaritons and their spectroscopic resonances can be actively controlled by temperature. This tunability originates from the effective change in local dielectric properties of the VO2 sublayer in the course of the temperature-tuned insulator-to-metal phase transition. The high susceptibility of polaritons to electronic phase transitions opens new possibilities for applications of vdW materials in combination with strongly correlated quantum materials.

2.
Nat Commun ; 7: 13079, 2016 10 07.
Article in English | MEDLINE | ID: mdl-27713412

ABSTRACT

Silk protein fibres produced by silkworms and spiders are renowned for their unparalleled mechanical strength and extensibility arising from their high-ß-sheet crystal contents as natural materials. Investigation of ß-sheet-oriented conformational transitions in silk proteins at the nanoscale remains a challenge using conventional imaging techniques given their limitations in chemical sensitivity or limited spatial resolution. Here, we report on electron-regulated nanoscale polymorphic transitions in silk proteins revealed by near-field infrared imaging and nano-spectroscopy at resolutions approaching the molecular level. The ability to locally probe nanoscale protein structural transitions combined with nanometre-precision electron-beam lithography offers us the capability to finely control the structure of silk proteins in two and three dimensions. Our work paves the way for unlocking essential nanoscopic protein structures and critical conditions for electron-induced conformational transitions, offering new rules to design protein-based nanoarchitectures.


Subject(s)
Fibroins/chemistry , Fibroins/ultrastructure , Silk/chemistry , Silk/ultrastructure , Animals , Bombyx/metabolism , Imaging, Three-Dimensional/methods , Molecular Conformation , Spectroscopy, Fourier Transform Infrared/methods , Spiders/metabolism
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