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Light Controlled Intracellular Protein Release: Tracking Ras Interactions With Superresolution Fluorescence Microscopy
Author(s) -
Yun Jason,
Phelps Carey,
Morales Demosthenes,
Nan Xiaolin,
Reich Norbert
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.801.3
Subject(s) - intracellular , chemistry , biophysics , gtpase , internalization , streptavidin , microbiology and biotechnology , biotin , cell , nanotechnology , biochemistry , biology , materials science
Although fusion proteins have been extremely helpful in the study of intracellular protein dynamics, this approach has significant drawbacks. We circumvent such problems by delivering dye‐conjugated proteins using our Nano‐optogenetic platform, which relies on hollow gold nanoshells to release proteins with NIR laser exposure. Herein, we report the delivery of a NS1 monobody, known to prevent dimerization of RAS GTPases that inhibits downstream signal transduction for cell division. Our modular nanoplatform is appended with thiol linked scaffolds containing a streptavidin‐biotin cell‐penetrating peptide for cell internalization and a nitriloacetic acid moiety to bind the polyhistidine dye‐labeled NS1 in the presence of copper. Near‐infrared laser activation allows for controlled spatio‐temporal endosomal release of the dye‐labeled NS1 to colocalize with RAS GTPase. Our approach can deliver any dye‐label His‐tagged protein of interest with controlled spatio‐temporal release inside cells. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .