ArticleACS sensors2018
Real-Time In Situ Secondary Structure Analysis of Protein Monolayer with Mid-Infrared Plasmonic Nanoantennas.
Article in ACS sensors, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Polarization-independent dielectric gradient near-perfect absorbers for aqueous mid-infrared molecular sensing.Npj nanophotonics · 2026Article
- Nanoplasmonic Infrared Microarray Sensor Enabling Structural Protein Biomarker-Based Drug Screening for Neurodegenerative Diseases.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Plasmon Enhanced IR Spectroelectrochemistry.ACS measurement science au · 2024Review
- Advancements and Perspectives in Optical Biosensors.ACS omega · 2024Review
- Wavelength multiplexing infrared metasurfaces for protein recognition and trace detection.Nanophotonics (Berlin, Germany) · 2023Article
- Research Progress in Surface-Enhanced Infrared Absorption Spectroscopy: From Performance Optimization, Sensing Applications, to System Integration.Nanomaterials (Basel, Switzerland) · 2023Review
- Artificial intelligence-coupled plasmonic infrared sensor for detection of structural protein biomarkers in neurodegenerative diseases.Science advances · 2023Article
- High-sensitivity hyperspectral vibrational imaging of heart tissues by mid-infrared photothermal microscopy.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2022Article
- Artificial Intelligence in Meta-optics.Chemical reviews · 2022Review
- Giant mid-IR resonant coupling to molecular vibrations in sub-nm gaps of plasmonic multilayer metafilms.Light, science & applications · 2022Article
- Opportunities and challenges of alpha-synuclein as a potential biomarker for Parkinson's disease and other synucleinopathies.NPJ Parkinson's disease · 2022Review
- Article
- Plasmonic Resonant Nanoantennas Induce Changes in the Shape and the Intensity of Infrared Spectra of Phospholipids.Molecules (Basel, Switzerland) · 2021Article
- Infrared Metasurface Augmented by Deep Learning for Monitoring Dynamics between All Major Classes of Biomolecules.Advanced materials (Deerfield Beach, Fla.) · 2021Article
- Adaptive Method for Quantitative Estimation of Glucose and Fructose Concentrations in Aqueous Solutions Based on Infrared Nanoantenna Optics.Sensors (Basel, Switzerland) · 2019Article
- Quantifying the Limits of Detection of Surface-Enhanced Infrared Spectroscopy with Grating Order-Coupled Nanogap Antennas.ACS photonics · 2018Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dynamic detection of protein conformational changes at physiological conditions on a minute amount of samples is immensely important for understanding the structural determinants of protein function in health and disease and to develop assays and diagnostics for protein misfolding and protein aggregation diseases. Herein, we experimentally demonstrate the capabilities of a mid-infrared plasmonic biosensor for real-time and in situ protein secondary structure analysis in aqueous environment at nanoscale. We present label-free ultrasensitive dynamic monitoring of β-sheet to disordered conformational transitions in a monolayer of the disease-related α-synuclein protein under varying stimulus conditions. Our experiments show that the extracted secondary structure signals from plasmonically enhanced amide I signatures in the protein monolayer can be reliably and reproducibly acquired with second derivative analysis for dynamic monitoring. Furthermore, by using a polymer layer we show that our nanoplasmonic approach of extracting the frequency components of vibrational signatures matches with the results attained from gold-standard infrared transmission measurements. By facilitating conformational analysis on small quantities of immobilized proteins in response to external stimuli such as drugs, our plasmonic biosensor could be used to introduce platforms for screening small molecule modulators of protein misfolding and aggregation.
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