ArticleNanomaterials (Basel, Switzerland)2020
Phosphorylation-Dependent SERS Readout for Activity Assay of Protein Kinase A in Cell Extracts.
Article in Nanomaterials (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 8 citations in OpenAlex.
- Label-Free SERS Sensors for Real-Time Monitoring of Tyrosine Phosphorylation.Analytical chemistry · 2024Article
- Positively-charged plasmonic nanostructures for SERS sensing applications.RSC advances · 2021Review
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8 authors at 4 institutions in 2 countries.
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Abstract
Protein kinases are key regulators of cell function, the abnormal activity of which may induce several human diseases, including cancers. Therefore, it is of great significance to develop a sensitive and reliable method for assaying protein kinase activities in real biological samples. Here, we report the phosphorylation-dependent surface-enhanced Raman scattering (SERS) readout of spermine-functionalized silver nanoparticles (AgNPs) for protein kinase A (PKA) activity assay in cell extracts. In this assay, the presence of PKA would phosphorylate and alter the net charge states of Raman dye-labeled substrate peptides, and the resulting anionic products could absorb onto the AgNPs with cationic surface charge through electrostatic attraction. Meanwhile, the Raman signals of dyes labeled on peptides were strongly enhanced by the aggregated AgNPs with interparticle hot spots formed in assay buffer. The SERS readout was directly proportional to the PKA activity in a wide range of 0.0001-0.5 U·μL
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