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Date
2013-09-11Type
- Journal Article
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Cited 46 times in
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Cited 47 times in
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Abstract
Fully exploiting the capability of nano-optics to enhance light-matter interaction on the nanoscale is conditioned by bringing the nano-object to interrogate within the minuscule volume where the field is concentrated. There currently exists several approaches to control the immobilization of nano-objects but they all involve a cumbersome delivery step and require prior knowledge of the “hot spot” location.1−6 Herein, we present a novel technique in which the enhanced local field in the hot spot is the driving mechanism that triggers the binding of proteins via three-photon absorption. This way, we demonstrate exclusive immobilization of nanoscale amounts of bovine serum albumin molecules into the nanometer-sized gap of plasmonic dimers. The immobilized proteins can then act as a scaffold to subsequently attach an additional nanoscale object such as a molecule or a nanocrystal. This universal technique is envisioned to benefit a wide range of nano-optical functionalities including biosensing,7−12 enhanced spectroscopy like surface-enhanced Raman spectroscopy13,14 or surface-enhanced infrared absorption spectroscopy,15 as well as quantum optics.1,2,6 (© 2013 American Chemical Society). Show more
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publishedExternal links
Journal / series
Nano LettersVolume
Pages / Article No.
Publisher
American Chemical SocietySubject
Nanopositioning; Fabrication; Plasmonics; Biosensing; Quantum opticsOrganisational unit
09698 - Quidant, Romain / Quidant, Romain
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Show all metadata
Citations
Cited 46 times in
Web of Science
Cited 47 times in
Scopus
ETH Bibliography
no
Altmetrics