Spectroscopic investigation of the ultrasound impacts on the molecular structures of blood proteins

Low-frequency ultrasound waves (LFUWs) are applied in various medical treatments, but their effects on blood proteins’ molecular structure are not well understood. This study explores how LFUWs alter blood protein structures, utilizing ultraviolet-visible (UV–vis), Raman, and Fourier transform infra...

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Main Authors: Aysh Y. Madkhli, Waad A. Al-Otaibi, Sahar M. AlMotwaa, Amal Mohsen Alghamdi, Norah T.S. Albogamy, Manal A. Babaker, Eida M. Alshammari, Mohammed J. Al Nahari, Abdu Saeed
Format: Article
Language:English
Published: Elsevier 2025-06-01
Series:Chemical Physics Impact
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Online Access:http://www.sciencedirect.com/science/article/pii/S2667022425000325
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author Aysh Y. Madkhli
Waad A. Al-Otaibi
Sahar M. AlMotwaa
Amal Mohsen Alghamdi
Norah T.S. Albogamy
Manal A. Babaker
Eida M. Alshammari
Mohammed J. Al Nahari
Abdu Saeed
author_facet Aysh Y. Madkhli
Waad A. Al-Otaibi
Sahar M. AlMotwaa
Amal Mohsen Alghamdi
Norah T.S. Albogamy
Manal A. Babaker
Eida M. Alshammari
Mohammed J. Al Nahari
Abdu Saeed
author_sort Aysh Y. Madkhli
collection DOAJ
description Low-frequency ultrasound waves (LFUWs) are applied in various medical treatments, but their effects on blood proteins’ molecular structure are not well understood. This study explores how LFUWs alter blood protein structures, utilizing ultraviolet-visible (UV–vis), Raman, and Fourier transform infrared (FTIR) spectroscopies. Blood samples from five volunteers were subjected to LFUWs for periods of 0, 5, 10, 15, and 20 min. Multivariate analyses, including hierarchical cluster analysis (HCA) and principal components analysis (PCA), were performed to distinguish between the spectroscopic data of control samples and those exposed to LFUWs. Results from UV–vis spectroscopy indicated hemolysis and changes in hemoglobin (Hb) and amino acids after more than 10 min of LFUW exposure. Raman spectroscopy showed a negative correlation between LFUW exposure time and intensity ratio, hinting at Hb deoxygenation and structural changes. FTIR spectroscopy revealed an increase in α-helices and a decrease in random coils, β-sheets, and turns in samples exposed to 10 min or more of sonication. These findings suggest that LFUW exposure could cause blood protein denaturation, likely through localized hyperthermia induced by ultrasound waves. This study highlights the potential of LFUWs to induce protein denaturation and demonstrates the effectiveness of UV–vis, Raman, and FTIR spectroscopy in investigating the impacts of ultrasound on biomolecular structures.
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spelling doaj-art-2638566cf7b144d899f74a961c142f982025-02-06T05:12:59ZengElsevierChemical Physics Impact2667-02242025-06-0110100844Spectroscopic investigation of the ultrasound impacts on the molecular structures of blood proteinsAysh Y. Madkhli0Waad A. Al-Otaibi1Sahar M. AlMotwaa2Amal Mohsen Alghamdi3Norah T.S. Albogamy4Manal A. Babaker5Eida M. Alshammari6Mohammed J. Al Nahari7Abdu Saeed8Jazan University, College of Science, Department of Physical Sciences, Physics Division, P.O. Box 114, Jazan, 45142, Saudi ArabiaDepartment of Chemistry, College of Science and Humanities, Shaqra University, Shaqra 15526, Saudi ArabiaDepartment of Chemistry, College of Science and Humanities, Shaqra University, Shaqra 15526, Saudi ArabiaPhysics department, Faculty of Science, King Khalid University, Abha 61411, Saudi ArabiaPhysics Department, University College-Taraba, Taif University, Al-Hawiah, Taif 21974, Saudi ArabiaDepartment of Chemistry, Faculty of Science, Majmaah University, Al Majmaah 11952, Saudi ArabiaDepartment of Chemistry, College of Sciences, University of Ha'il, Ha'il 2440, Saudi ArabiaDepartment of Medicine and Surgery, Batterjee Medical College, Jeddah 21589, Saudi ArabiaDepartment of Physics, Faculty of Science, King Abdulaziz University, Jeddah 21589, Saudi Arabia; Department of Physics, Thamar University, Thamar 87246, Yemen; Corresponding author.Low-frequency ultrasound waves (LFUWs) are applied in various medical treatments, but their effects on blood proteins’ molecular structure are not well understood. This study explores how LFUWs alter blood protein structures, utilizing ultraviolet-visible (UV–vis), Raman, and Fourier transform infrared (FTIR) spectroscopies. Blood samples from five volunteers were subjected to LFUWs for periods of 0, 5, 10, 15, and 20 min. Multivariate analyses, including hierarchical cluster analysis (HCA) and principal components analysis (PCA), were performed to distinguish between the spectroscopic data of control samples and those exposed to LFUWs. Results from UV–vis spectroscopy indicated hemolysis and changes in hemoglobin (Hb) and amino acids after more than 10 min of LFUW exposure. Raman spectroscopy showed a negative correlation between LFUW exposure time and intensity ratio, hinting at Hb deoxygenation and structural changes. FTIR spectroscopy revealed an increase in α-helices and a decrease in random coils, β-sheets, and turns in samples exposed to 10 min or more of sonication. These findings suggest that LFUW exposure could cause blood protein denaturation, likely through localized hyperthermia induced by ultrasound waves. This study highlights the potential of LFUWs to induce protein denaturation and demonstrates the effectiveness of UV–vis, Raman, and FTIR spectroscopy in investigating the impacts of ultrasound on biomolecular structures.http://www.sciencedirect.com/science/article/pii/S2667022425000325UltrasoundBlood proteinMolecular structureUV-visible specroscopyRaman spectroscopyFTIR
spellingShingle Aysh Y. Madkhli
Waad A. Al-Otaibi
Sahar M. AlMotwaa
Amal Mohsen Alghamdi
Norah T.S. Albogamy
Manal A. Babaker
Eida M. Alshammari
Mohammed J. Al Nahari
Abdu Saeed
Spectroscopic investigation of the ultrasound impacts on the molecular structures of blood proteins
Chemical Physics Impact
Ultrasound
Blood protein
Molecular structure
UV-visible specroscopy
Raman spectroscopy
FTIR
title Spectroscopic investigation of the ultrasound impacts on the molecular structures of blood proteins
title_full Spectroscopic investigation of the ultrasound impacts on the molecular structures of blood proteins
title_fullStr Spectroscopic investigation of the ultrasound impacts on the molecular structures of blood proteins
title_full_unstemmed Spectroscopic investigation of the ultrasound impacts on the molecular structures of blood proteins
title_short Spectroscopic investigation of the ultrasound impacts on the molecular structures of blood proteins
title_sort spectroscopic investigation of the ultrasound impacts on the molecular structures of blood proteins
topic Ultrasound
Blood protein
Molecular structure
UV-visible specroscopy
Raman spectroscopy
FTIR
url http://www.sciencedirect.com/science/article/pii/S2667022425000325
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