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A Highly Specific Gold Nanoprobe for Live-Cell Single-Molecule Imaging

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LP2N, Université de Bordeaux, Institut d’Optique & CNRS UMR 5298, F- 33405 Talence, France
Laboratoire d’Enzymologie et Biochimie Structurales UPR3082, CNRS, F-91198 Gif-sur-Yvette France
§ Department of Cell Physiology and Metabolism, Centre Médical Universitaire, University of Geneva, Geneva, Switzerland
Université de Bordeaux, IINS UMR 5297, CNRS, F-33000 Bordeaux, France
Cite this: Nano Lett. 2013, 13, 4, 1489–1494
Publication Date (Web):March 4, 2013
https://doi.org/10.1021/nl304561g
Copyright © 2013 American Chemical Society

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    Abstract

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    Single molecule tracking in live cells is the ultimate tool to study subcellular protein dynamics, but it is often limited by the probe size and photostability. Because of these issues, long-term tracking of proteins in confined and crowded environments, such as intracellular spaces, remains challenging. We have developed a novel optical probe consisting of 5 nm gold nanoparticles functionalized with a small fragment of camelid antibodies that recognize widely used green fluorescent proteins (GFPs) with a very high affinity, which we call GFP-nanobodies. These small gold nanoparticles can be detected and tracked using photothermal imaging for arbitrarily long periods of time. Surface and intracellular GFP-proteins were effectively labeled even in very crowded environments such as adhesion sites and cytoskeletal structures both in vitro and in live cell cultures. These nanobody-coated gold nanoparticles are probes with unparalleled capabilities; small size, perfect photostability, high specificity, and versatility afforded by combination with the vast existing library of GFP-tagged proteins.

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