In-situ ultra-sensitive infrared absorption spectroscopy of biomolecule interactions in real time with plasmonic nanoantennas
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Infrared absorption spectroscopy is a powerful biochemical analysis tool as it extracts detailed molecular structural information in a label-free fashion. Its molecular specificity renders the technique sensitive to the subtle conformational changes exhibited by proteins in response to a variety of stimuli. Yet, sensitivity limitations and the extremely strong absorption bands of liquid water severely limit infrared spectroscopy in performing kinetic measurements in biomolecules’ native, aqueous environments. Here we demonstrate a plasmonic chip-based technology that overcomes these challenges, enabling the in-situ monitoring of protein and nanoparticle interactions at high sensitivity in real time, even allowing the observation of minute volumes of water displacement during binding events. Our approach leverages the plasmonic enhancement of absorption bands in conjunction with a non-classical form of internal reflection. These features not only expand the reach of infrared spectroscopy to a new class of biological interactions but also additionally enable a unique chip-based technology. Infrared absorption spectroscopy provides important information about molecules, but is hampered by the absorption of water. Adato and Altug exploit the plasmonic enhancement from nanoantennas to overcome this, enabling chip-based monitoring of biological samples in aqueous environments.
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The amplification effect caused by strong plasmon-molecule coupling between plasmonic resonance and molecular vibration is well-explained by temporal coupled-mode theory (TCMT).
“This amplification effect caused by the strong plasmon-molecule coupling between plasmonic resonance and molecular vibration was well-explained by temporal coupled-mode theory (TCMT)14,15.”
From Wavelength-multiplexed hook nanoantennas for machine learning enabled mid-infrared spectroscopy (2022) · cites this paper as [14]
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Advances in Nanoengineered Terahertz Technology: Generation, Modulation, and Bio-Applications
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Multispectral Cesaro-Type Fractal Plasmonic Nanoantennas
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- Authors
- Adato, R., & Altug, H.
- Affiliations
- École Polytechnique Fédérale de Lausanne (CH)
- Boston University (US)
- Corresponding author
- Altug, Hatice
- ORCID
- Altug, Hatice
- Venue
- Nature Communications
- Published
- 2013-07-23
- Volume
- 4
- Issue
- 1
- Pages
- 2154-2154
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC3759039
- OpenAlex
- W2059396803
- Cited by
- 406
- References
- 53
- Citations by year
- 2026: 17 · 2025: 26 · 2024: 26 · 2023: 19 · 2022: 23 · 2021: 34 · 2020: 33 · 2019: 40 · 2018: 41 · 2017: 42 · 2016: 47 · 2015: 34 · 2014: 19 · 2013: 5
- FWCI
- 19.33
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Nature Communications (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Funders
- National Science Foundation (0954790, CAREER)
- Office of Naval Research
- Division of Electrical, Communications and Cyber Systems
- Topics
- Physical Sciences › Engineering › Biomedical Engineering › Plasmonic and Surface Plasmon Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Spectroscopy Techniques in Biomedical and Chemical Research
- Physical Sciences › Materials Science › Electronic, Optical and Magnetic Materials › Gold and Silver Nanoparticles Synthesis and Applications
- Keywords
- infrared absorption spectroscopy, plasmonic nanoantennas, plasmonic enhancement, nanoparticle-protein interactions, protein conformational change, water absorption, in situ monitoring, binding kinetics, label-free detection
- MeSH terms
- Immunoassay, Kinetics, Proteins, Spectrophotometry, Infrared, Water, Protein Array Analysis, Nanostructures
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