Quantum Defect Sensitization via Phase-Changing Supercharged Antibody Fragments

Quantum defects in single-walled carbon nanotubes promote exciton localization, which enables potential applications in biodevices and quantum light sources. However, the effects of local electric fields on the emissive energy states of quantum defects and how they can be controlled are unexplored....

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Veröffentlicht in:Journal of the American Chemical Society 2024-05, Vol.146 (18), p.12454-12462
Hauptverfasser: Kim, Mijin, McCann, James J., Fortner, Jacob, Randall, Ewelina, Chen, Chen, Chen, Yu, Yaari, Zvi, Wang, YuHuang, Koder, Ronald L., Heller, Daniel A.
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Sprache:eng
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Zusammenfassung:Quantum defects in single-walled carbon nanotubes promote exciton localization, which enables potential applications in biodevices and quantum light sources. However, the effects of local electric fields on the emissive energy states of quantum defects and how they can be controlled are unexplored. Here, we investigate quantum defect sensitization by engineering an intrinsically disordered protein to undergo a phase change at a quantum defect site. We designed a supercharged single-chain antibody fragment (scFv) to enable a full ligand-induced folding transition from an intrinsically disordered state to a compact folded state in the presence of a cytokine. The supercharged scFv was conjugated to a quantum defect to induce a substantial local electric change upon ligand binding. Employing the detection of a proinflammatory biomarker, interleukin-6, as a representative model system, supercharged scFv-coupled quantum defects exhibited robust fluorescence wavelength shifts concomitant with the protein folding transition. Quantum chemical simulations suggest that the quantum defects amplify the optical response to the localization of charges produced upon the antigen-induced folding of the proteins, which is difficult to achieve in unmodified nanotubes. These findings portend new approaches to modulate quantum defect emission for biomarker sensing and protein biophysics and to engineer proteins to modulate binding signal transduction.
ISSN:0002-7863
1520-5126
1520-5126
DOI:10.1021/jacs.4c00149