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Creators/Authors contains: "Deiters, Alexander"

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  1. ; ; ; (, RSC Chemical Biology)
    We report targeted protein degradation through the site-specific recruitment of native ubiquitin ligases to a protein of interestviaconjugation of E3 ligase ligands. 
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  2. ; ; ; ; (, ACS Synthetic Biology)
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  3. ; (, Current Opinion in Chemical Biology)
    null (Ed.)
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  4. ; ; (, Journal of the American Chemical Society)
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  5. ; ; ; (, Chemical Science)
    Chemically induced dimerization of FKBP and FRB using rapamycin and rapamycin analogs has been utilized in a variety of biological applications. Formation of the FKBP-rapamycin-FRB ternary complex is typically used to activate a biological process and this interaction has proven to be essentially irreversible. In many cases, it would be beneficial to also have temporal control over deactivating a biological process once it has been initiated. Thus, we developed the first reactive oxygen species-generating rapamycin analog toward this goal. The BODIPY-rapamycin analog BORap is capable of dimerizing FKBP and FRB to form a ternary complex, and upon irradiation with 530 nm light, generates singlet oxygen to oxidize and inactivate proteins of interest fused to FKBP/FRB. 
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  6. ; ; ; ; (, Chemical Science)
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    Due to their high stability and specificity in living cells, fluorescently labeled nanobodies are perfect probes for visualizing intracellular targets at an endogenous level. However, intrabodies bind unrestrainedly and hence may interfere with the target protein function. Here, we report a strategy to prevent premature binding through the development of photo-conditional intrabodies. Using genetic code expansion, we introduce photocaged amino acids within the nanobody-binding interface, which, after photo-activation, show instantaneous binding of target proteins with high spatiotemporal precision inside living cells. Due to the highly stable binding, light-guided intrabodies offer a versatile platform for downstream imaging and regulation of target proteins. 
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