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Protein Conformational Changes in Breast Cancer Sera Using Infrared Spectroscopic Analysis.
Cancers (Basel). 2020 Jun 27; 12(7)C

Abstract

Protein structural alterations, including misfolding and aggregation, are a hallmark of several diseases, including cancer. However, the possible clinical application of protein conformational analysis using infrared spectroscopy to detect cancer-associated structural changes in proteins has not been established yet. The present study investigates the applicability of Fourier transform infrared spectroscopy in distinguishing the sera of healthy individuals and breast cancer patients. The cancer-associated alterations in the protein structure were analyzed by fitting the amide I (1600-1700 cm-1) band of experimental curves, as well as by comparing the ratio of the absorbance values at the amide II and amide III bands, assigning those as the infrared spectral signatures. The snapshot of the breast cancer-associated alteration in circulating DNA and RNA was also evaluated by extending the spectral fitting protocol to the complex region of carbohydrates and nucleic acids, 1140-1000 cm-1. The sensitivity and specificity of these signatures, representing the ratio of the α-helix and β-pleated sheet in proteins, were both 90%. Likewise, the ratio of amides II and amide III (I1556/I1295) had a sensitivity and specificity of 100% and 80%, respectively. Thus, infrared spectroscopy can serve as a powerful tool to understand the protein structural alterations besides distinguishing breast cancer and healthy serum samples.

Authors+Show Affiliations

Department of Physics and Astronomy, Georgia State University, Atlanta, GA 30303, USA.Department of Biology, Georgia State University, Atlanta, GA 30303, USA.Department of Pathology, Stavanger University Hospital, Stavanger NO-4068, Norway.Department of Pathology, Emory University School of Medicine, Atlanta, GA 30322, USA.Department of Mathematics and Statistics, Georgia State University, Atlanta, GA 30303, USA.Department of Biology, Georgia State University, Atlanta, GA 30303, USA. Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, USA.Department of Physics and Astronomy, Georgia State University, Atlanta, GA 30303, USA. Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, USA.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

32605072

Citation

Ghimire, Hemendra, et al. "Protein Conformational Changes in Breast Cancer Sera Using Infrared Spectroscopic Analysis." Cancers, vol. 12, no. 7, 2020.
Ghimire H, Garlapati C, Janssen EAM, et al. Protein Conformational Changes in Breast Cancer Sera Using Infrared Spectroscopic Analysis. Cancers (Basel). 2020;12(7).
Ghimire, H., Garlapati, C., Janssen, E. A. M., Krishnamurti, U., Qin, G., Aneja, R., & Perera, A. G. U. (2020). Protein Conformational Changes in Breast Cancer Sera Using Infrared Spectroscopic Analysis. Cancers, 12(7). https://doi.org/10.3390/cancers12071708
Ghimire H, et al. Protein Conformational Changes in Breast Cancer Sera Using Infrared Spectroscopic Analysis. Cancers (Basel). 2020 Jun 27;12(7) PubMed PMID: 32605072.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Protein Conformational Changes in Breast Cancer Sera Using Infrared Spectroscopic Analysis. AU - Ghimire,Hemendra, AU - Garlapati,Chakravarthy, AU - Janssen,Emiel A M, AU - Krishnamurti,Uma, AU - Qin,Gengsheng, AU - Aneja,Ritu, AU - Perera,A G Unil, Y1 - 2020/06/27/ PY - 2020/05/26/received PY - 2020/06/19/revised PY - 2020/06/25/accepted PY - 2020/7/2/entrez KW - ATR-FTIR KW - breast cancer biomarkers KW - infrared spectroscopy KW - protein secondary structure KW - serum KW - spectral deconvolution JF - Cancers JO - Cancers (Basel) VL - 12 IS - 7 N2 - Protein structural alterations, including misfolding and aggregation, are a hallmark of several diseases, including cancer. However, the possible clinical application of protein conformational analysis using infrared spectroscopy to detect cancer-associated structural changes in proteins has not been established yet. The present study investigates the applicability of Fourier transform infrared spectroscopy in distinguishing the sera of healthy individuals and breast cancer patients. The cancer-associated alterations in the protein structure were analyzed by fitting the amide I (1600-1700 cm-1) band of experimental curves, as well as by comparing the ratio of the absorbance values at the amide II and amide III bands, assigning those as the infrared spectral signatures. The snapshot of the breast cancer-associated alteration in circulating DNA and RNA was also evaluated by extending the spectral fitting protocol to the complex region of carbohydrates and nucleic acids, 1140-1000 cm-1. The sensitivity and specificity of these signatures, representing the ratio of the α-helix and β-pleated sheet in proteins, were both 90%. Likewise, the ratio of amides II and amide III (I1556/I1295) had a sensitivity and specificity of 100% and 80%, respectively. Thus, infrared spectroscopy can serve as a powerful tool to understand the protein structural alterations besides distinguishing breast cancer and healthy serum samples. SN - 2072-6694 UR - https://www.unboundmedicine.com/medline/citation/32605072/Protein_Conformational_Changes_in_Breast_Cancer_Sera_Using_Infrared_Spectroscopic_Analysis DB - PRIME DP - Unbound Medicine ER -
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