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Título: | Quantum dot−peptide conjugates as energy transfer probes for sensing the proteolytic activity of matrix metalloproteinase-14 |
Autor: | Jin, Zhicheng; Dridi, Narjes; Palui, Goutam; Palomo, Valle CSIC ORCID ; Jokerst, Jesse V.; Dawson, Philip E.; Sang, Qing-Xiang Amy; Mattoussi, Hedi | Fecha de publicación: | 27-ene-2023 | Editor: | American Chemical Society | Citación: | Analytical Chemistry 95 (5) 2713–2722 (2023) | Resumen: | We detail the assembly and characterization of quantum dot (QD)−dye conjugates constructed using a peptide bridge specifically designed to recognize and interact with a breast cancer biomarker─matrix metalloproteinase-14 (MMP-14). The assembled QD conjugates are then used as optically addressable probes, relying on Förster resonance energy transfer (FRET) interactions as a transduction mechanism to detect the activity of MMP-14 in solution phase. The QDs were first coated with dithiolane poly(ethylene glycol) (PEG) bearing a carboxyl group that allows coupling via amide bond formation with different dye-labeled peptides. The analytical capability of the conjugates is enabled by correlating changes in the FRET efficiency with the conjugate valence and/or QD-to-dye separation distance, triggered and modulated by enzymatic proteolysis of surface-tethered peptides. The FRET probe exhibits great sensitivity to enzyme digestion with sub-nanomolar limit of detection. We further analyze the proteolysis data within the framework of the Michaelis–Menten model, which considers the fact that surface-attached peptides have a slower diffusion coefficient than free peptides. This results in reduced collision frequency and lower catalytic efficiency, kcat/KM. Our results suggest that our conjugate design is promising, effective, and potentially useful for in vivo analysis. | Descripción: | 10 p.-5 fig.-2 tab. 1 graph. abst. | Versión del editor: | https://doi.org/10.1021/acs.analchem.2c03400 | URI: | http://hdl.handle.net/10261/355497 | DOI: | 10.1021/acs.analchem.2c03400 | ISSN: | 0003-2700 | E-ISSN: | 1520-6882 |
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