It is a well-established fact that iron metabolism is disrupted in breast cancer cells. Assessment of iron transport and metabolism is necessary to understand molecular mechanism of breast cancer progression. Previously, Raman spectroscopy has been used to measure the Raman spectral profile of iron-bound proteins in breast cancer cells. By harnessing the principle of inelastic scattering of light, Raman spectroscopy offers a powerful, label-free, and nondestructive tool for determination of molecular structures and analysis of chemical bonds. The current study employed a specific experimental approach to capture shifts in the Raman signature of iron-binding proteins, such as transferrin. Focusing on cytoplasmic regions (exclusive of the nucleus) permits improved analysis of iron-binding proteins localized to vesicles present in the cytoplasm. The acquired spectra were subjected to rigorous analysis using singular value decomposition (SVD), a powerful mathematical technique that possesses the ability to reveal underlying trends and enhance biological analysis and interpretation. It involves detecting overlapping frequency patterns in the dataset. By applying SVD to distinguish the Raman spectral profiles of iron-bound transferrin in breast cancer cells, we obtained accurate results that have played a pivotal role in discerning and characterizing the Raman spectral profile of iron-bound transferrin in breast cancer cells.
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