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Investigation on thyroglobulin and myoglobin using graphene-enhanced Raman spectroscopy as a tool.
Anamika Sharma1, Venkata Ramanaiah Dantham1
1Department of Physics, Indian Institute of Technology Patna, Bihar, India, 801103. dantham@iitp.ac.in.
Nanoscale
|July 10, 2025
Summary
Graphene-enhanced Raman spectroscopy significantly improves the detection of vibrational modes for thyroglobulin (Tg) and myoglobin (Mb), enabling detailed protein analysis. This advanced technique overcomes limitations of conventional Raman spectroscopy for these important biomarkers.
Area of Science:
- Biophysics
- Spectroscopy
- Materials Science
Background:
- Thyroglobulin (Tg) is crucial for thyroid hormone production.
- Myoglobin (Mb) serves as an early biomarker for cardiac events.
- Conventional Raman spectroscopy often yields weak signals for biological molecules.
Purpose of the Study:
- To investigate thyroglobulin (Tg) and myoglobin (Mb) using graphene-enhanced Raman spectroscopy (GERS).
- To compare GERS with conventional Raman spectroscopy (CRS) for protein analysis.
- To assign vibrational modes observed in GERS spectra of Tg and Mb.
Main Methods:
- UV-visible spectrophotometry for absorption properties.
- Drop-casting of 1 μM Tg and Mb solutions onto glass substrates.
- Acquisition of conventional Raman scattering (CRS) and graphene-enhanced Raman scattering (GERS) spectra.
Main Results:
- CRS spectra showed insignificant vibrational modes for Tg and Mb.
- GERS spectra provided a high signal-to-noise ratio for both proteins.
- The intensity and number of vibrational modes in GERS spectra were location-dependent.
Conclusions:
- Graphene-enhanced Raman spectroscopy is a powerful tool for analyzing proteins like Tg and Mb.
- GERS significantly enhances the detection of weak vibrational signals compared to CRS.
- Detailed assignment of vibrational modes in GERS spectra was achieved.
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