Mycobacteria outer membrane, which is rich in lipids and important disaccharide precursors such as trehalose, has been the prime target for drug development against tuberculosis. We have shown that trehalose, when conjugated to nanoparticles, led to specific interactions with mycobacteria, and nanoparticle-based drug delivery systems exhibited enhanced antibacterial activity due to functionalization with trehalose. However, the mechanism of how trehalose mediates the interactions of nanoparticles with mycobacteria is not well understood. To investigate this, we developed a trehalose-functionalized photoaffinity nanoprobe that could photo-crosslink the protein receptor on mycobacteria. Our nanoprobe could magnetically isolate the trehalose-bound protein complex without additional affinity purification. The synthesis of the photoaffinity trehalose-functionalized nanoprobe, the capture, isolation, and identification of the protein receptor will be presented. This method is expected to facilitate the detection of receptors expressed in other bacterial species or human cells by simply changing the ligand.

Development of a trehalose-functionalized photoaffinity nanoprobe to capture trehalose-binding proteins on mycobacteria

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ACS Fall 2022

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