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SUMMARY:CLONABLE SELENIUM NANOPARTICLES: IN SITU PROTEIN LABELING FOR  BIOL
 OGICAL MICROSCOPY
LOCATION:Virtual Research Seminar
TZID:America/Denver
DTSTART:20209101T000000
UID:2026-04-24-11-01-41@natsci.colostate.edu
DTSTAMP:20260424T110141
Description:Biological microscopic studies\, once revolutionized by the dis
 covery of clonable fluorophores like Green Fluorescent Protein (GFP)\, eng
 ender foundational evidence for cellular processes via in situ protein lab
 eling and tracking by fluorescence. As light microscopy is inherently diff
 raction limited\, electron microscopy (EM) unveils details of cellular ult
 rastructure with nanometer scale resolution. The primary challenge of biol
 ogical EM is generating target specific contrast. While methods have been 
 developed to create targeted contrast\, none have achieved the specificity
  of an encodable label. We developed a clonable nanoparticle by isolating 
 a metalloid reductase from a selenophilic plant capable of reducing seleno
 oxyanion precursors into zero valent\, amorphous Se nanoparticles (SeNPs).
  After demonstrating the portability of the enzyme across species through 
 the maintenance of its activity in vitro and in vivo\, modification of the
  wild type further enhanced its performance as a clonable selenium nanopar
 ticle (cSeNP) tag. We then used the recombinant enzyme in a proof of conce
 pt study that involved tracking filamenting protein FtsZ in vivo. Once we 
 expressed the cSeNP-FtsZ chimera in E. coli\, electron micrographs mimicke
 d fluorescence images from studies of GFP-FtsZ fusions. In addition\, we e
 xplored the possibilities of using the enzyme to synthesize metal selenide
  quantum dots (QDs). We have used both a bottom-up and a top-down approach
  to synthesize QDs in vitro\, and we continue to develop the protocols for
  in vivo correlative labeling applications. We continue to optimize establ
 ished preservation and imaging methods to be compatible with clonable nano
 particle technology and to discover other reductases from our library of c
 andidate species.\n\n&nbsp\;\n\n&nbsp\;\n\n&nbsp\; 4:00 pm
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