NDLI: Multicolored nanometre-resolution mapping of single protein–ligand binding complexes using far-field photostable optical nanoscopy (PHOTON)

Content Provider	Royal Society of Chemistry (RSC)
Author	Xu, Xiao-Hong Nancy Huang, Tao
Copyright Year	2011
Abstract	Mapping of individual ligand molecules and their binding sites in single protein–ligand complexes at nanometer resolution in real-time would enable probing their structures and functions in vitro and in vivo. In this study, we have developed far-field photostable optical nanoscopy (PHOTON) for mapping single ligand molecules (biotin) and their binding sites in individual protein–ligand complexes (streptavidin–biotin) with 1.2 nm spatial resolution and 100 ms temporal resolution. PHOTON includes one standard far-field optical microscope with a halogen-lamp illuminator; single-molecule-nanoparticle-optical-biosensors (SMNOBS) with exceptionally high quantum-yield (QY) of Rayleigh scattering and photostability (non-photobleaching, non-photoblinking) as imaging probes; and Multispectral Imaging System (MSIS) for spectral isolation of individual SMNOBS with 1 nm wavelength resolution. Intrinsic size- and shape- dependent localized-surface-plasmon-resonance (LSPR) spectra of single SMNOBS provide multiple-spectral (color) nanoprobes for sub-diffraction imaging, offering feasibility of probing of binding structures and functions of single protein–ligand complexes at nm (potentially achieving Ångstrom) resolution in real-time.
Starting Page	3567
Ending Page	3572
Page Count	6
File Format	HTM / HTML PDF
ISSN	20403364
Volume Number	3
Issue Number	9
Journal	Nanoscale
DOI	10.1039/c1nr10182j
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Rayleigh scattering Ligand Optical microscope Nanometre Ångström Biotin Wavelength Rayleigh
Content Type	Text
Resource Type	Article
Subject	Nanoscience and Nanotechnology

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