4.8 Article

DNA-Programed Plasmon Rulers Decrypt Single-Receptor Dimerization on Cell Membrane

Journal

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 145, Issue 2, Pages 1273-1284

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/jacs.2c11201

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Real-time observation of receptor tyrosine kinases family (RTKs) at single-molecule level based on plasmon rulers enables precise regulation and dynamic monitoring of dimerization process. These nanoprobes show substantial application in regulating RTKs protein dimerization/phosphorylation and activating downstream signaling pathways.
Decrypting the dynamics of receptor dimerization on cell membranes bears great importance in identifying the mechanisms regulating diverse cellular activities. In this regard, long-term monitoring of single-molecule behavior during receptor dimerization allows deepening insight into the dimerization process and tracking of the behavior of individual receptors, yet this remains to be realized. Herein, real-time observation of the receptor tyrosine kinases family (RTKs) at single-molecule level based on plasmon rulers was achieved for the first time, which enabled precise regulation and dynamic monitoring of the dimerization process by DNA programming with excellent photostability. Additionally, those nanoprobes demonstrated substantial application in the regulation of RTKs protein dimerization/phosphorylation and activation of downstream signaling pathways. The proposed nanoprobes hold considerable potential for elucidating the molecular mechanisms of single-receptor dimerization as well as the conformational transitions upon dimerization, providing a new paradigm for the precise manipulation and monitoring of specific single-receptor crosslink events in biological systems.

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