International Journal of Biomedicine (Dec 2022)

Leading–Edge Portable Biosensors and Biomarkers Development for Raman Biospectroscopy and Imaging in Cancer Diagnosis

  • Alireza Heidari,
  • Zahra Torfeh,
  • Sophia Iorgulescu,
  • Olivia Robinson,
  • Lin Hu,
  • Charlotte Vauclin,
  • Ntalie Schiltz,
  • Scarlett Sondermann,
  • Lucy MacLennan,
  • Julia Smith,
  • Lydia Williamson

DOI
https://doi.org/10.21103/Article12(4)_RA1
Journal volume & issue
Vol. 12, no. 4
pp. 493 – 505

Abstract

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Raman spectroscopy is an important method for identifying molecules, which is widely used in determining the chemical and structural characteristics of various substances. Many materials have a special Raman spectrum, so that this phenomenon has turned the Raman device into an efficient tool for studying the structural and chemical properties of molecules. Since it is possible to obtain detailed information about the chemical and structural characteristics of biological compounds from Raman spectroscopy, the use of this method is rapidly expanding in the field of life sciences, especially in biological and medical studies. There is no need for special, time–consuming and expensive preparations in the study of materials with the help of a Raman device. In the protein Raman spectrum, distinct bands arise from the vibrational states of the peptide backbone and amino acid side chains. Therefore, based on the position and intensity of the protein's Raman spectrum, it is possible to obtain valuable information about its second, third, and fourth structures. Also, the Raman spectrum of the protein contains information about the orientation and surrounding environment of the amino acid side chains. The correct formation of the disulfide bond in the protein structure can also be studied with the help of the Raman device. In general, the Raman spectrum of proteins contains multiple discrete bands that represent the vibrational states of the molecule and is used as a selective fingerprint to accurately determine the three–dimensional structure of proteins, intramolecular dynamics, and intermolecular interactions.

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