Resonant plasmonic nanoslits enable in vitro observation of single-monolayer collagen-peptide dynamics
Proteins perform a variety of essential functions in living cells and thus are of critical interest for drug delivery as well as disease biomarkers. The different functions are derived from a hugely diverse set of structures, fueling interest in their conformational states. Surface-enhanced infrared...
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| Main Authors: | , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
May 28, 2019
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| In: |
ACS sensors
Year: 2019, Volume: 4, Issue: 8, Pages: 1966-1972 |
| ISSN: | 2379-3694 |
| DOI: | 10.1021/acssensors.9b00377 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1021/acssensors.9b00377
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| Author Notes: | Rostyslav Semenyshyn, Mario Hentschel, Christian Huck, Jochen Vogt, Felix Weiher, Harald Giessen, and Frank Neubrech |
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| 245 | 1 | 0 | |a Resonant plasmonic nanoslits enable in vitro observation of single-monolayer collagen-peptide dynamics |c Rostyslav Semenyshyn, Mario Hentschel, Christian Huck, Jochen Vogt, Felix Weiher, Harald Giessen, and Frank Neubrech |
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| 520 | |a Proteins perform a variety of essential functions in living cells and thus are of critical interest for drug delivery as well as disease biomarkers. The different functions are derived from a hugely diverse set of structures, fueling interest in their conformational states. Surface-enhanced infrared absorption spectroscopy has been utilized to detect and discriminate protein monomers. As an important step forward, we are investigating collagen peptides consisting of a triple helix. While they constitute the main structural building blocks in many complex proteins, they are also a perfect model system for the complex proteins relevant in biological systems. Their complex spectroscopic information as well as the overall small size present a significant challenge for their detection and discrimination. Using resonant plasmonic nanoslits, which are known to show larger specificity compared to nanoantennas, we overcome this challenge. We perform in vitro surface-enhanced absorption spectroscopy studies and track the conformational changes of these collagen peptides under two different external stimuli, which are temperature and chemical surroundings. Modeling the coupling between the amide I vibrational modes and the plasmonic resonance, we can extract the conformational state of the collages and thus monitor the folding and unfolding dynamics of even a single monolayer. This leads to new prospects in studies of single layers of proteins and their folding behavior in minute amounts in a living environment. | ||
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