ArticleScientific reports2018
Triggering molecular assembly at the mesoscale for advanced Raman detection of proteins in liquid.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed.
- Ion-exchanged glass microrods as hybrid SERS/fluorescence substrates for molecular beacon-based DNA detection.Analytical and bioanalytical chemistry · 2021Article
- Cost Effective Silver Nanowire-Decorated Graphene Paper for Drop-On SERS Biodetection.Nanomaterials (Basel, Switzerland) · 2021Article
- Contributions of Molecular and Optical Techniques to the Clinical Diagnosis of Alzheimer's Disease.Brain sciences · 2020Review
- Hollow core photonic crystal fiber-assisted Raman spectroscopy as a tool for the detection of Alzheimer's disease biomarkers.Journal of biomedical optics · 2020Article
- Nanoscopic insights into the surface conformation of neurotoxic amyloid β oligomers.RSC advances · 2020Article
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5 authors.
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Abstract
An advanced optofluidic system for protein detection based on Raman signal amplification via dewetting and molecular gathering within temporary mesoscale assemblies is presented. The evaporation of a microliter volume of protein solution deposited in a circular microwell precisely follows an outward-receding geometry. Herein the combination of liquid withdrawal with intermolecular interactions induces the formation of self-assembled molecular domains at the solid-liquid interface. Through proper control of the evaporation rate, amplitude of the assemblies and time for spectral collection at the liquid edge are extensively raised, resulting in a local enhancement and refinement of the Raman response, respectively. Further signal amplification is obtained by taking advantage of the intense local electromagnetic fields generated upon adding a plasmonic coating to the microwell. Major advantages of this optofluidic method lie in the obtainment of high-quality, high-sensitivity Raman spectra with detection limit down to sub-micromolar values. Peculiarly, the assembled proteins in the liquid edge region maintain their native-like state without displaying spectral changes usually occurring when dried drop deposits are considered.
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