AI Article Synopsis
- Tip-enhanced Raman spectroscopy (TERS) allows researchers to examine biological surfaces at a nanometer scale, making it a valuable technique for studying proteins like insulin.
- The study reported distinct TER spectra from an insulin fibril, a cast film of protein, and a peptide microcrystal, revealing that surface roughness significantly affects the spectral outcomes.
- Two mechanisms for the enhanced Raman scattering were proposed, based on the observed low-intensity spectra from smooth surfaces and high-intensity, variable spectra from rough edges, suggesting different interactions at the molecular level.
Article Abstract
Tip-enhanced Raman spectroscopy (TERS) is a powerful tool for probing the surface of biological species with nanometer spatial resolution. Here, we report the TER spectra of an individual insulin fibril, the protein cast film and a short peptide (LVEALYL) microcrystal mimicking the fibril core. Two different types of TER spectra were acquired depending on the "roughness" of the probed surface at the molecular level. A fully reproducible, low-intensity, normal Raman-type spectrum was characteristic of the top flat surface of the microcrystal while highly variable, higher intensity TER spectra were obtained for the edges of the microcrystal, cast film, and fibril. As a result, two tip enhancement mechanisms of Raman scattering, long- and short-range, were proposed by analogy with the physical and chemical enhancement mechanisms, respectively, known for surface-enhanced Raman spectroscopy.
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| http://dx.doi.org/10.1177/0003702816651890 | DOI Listing |
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