Studies of Thyroid Hormones (Propylthiouracil and L-Thyroxine) Interaction with Human Serum Albumin-Spectroscopic Approach

Israa Ismail Abu Katteh; Husain Rashad Alsamamra; Musa Mahmoud Abu Teir

doi:doi:10.11648/j.ejb.20231101.11

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Studies of Thyroid Hormones (Propylthiouracil and L-Thyroxine) Interaction with Human Serum Albumin-Spectroscopic Approach

Israa Ismail Abu Katteh, Husain Rashad Alsamamra, Musa Mahmoud Abu Teir

Published in European Journal of Biophysics (Volume 11, Issue 1)

Received: 25 February 2023 Accepted: 21 March 2023 Published: 31 March 2023

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Abstract

In this work, UV-absorption, fluorescence spectroscopy and Fourier transform infrared (FTIR) spectroscopy were used to investigate the relationship between Propylthiouracil and L-Thyroxine with human serum albumin. The binding constants of propylthiouracil and L-Thyroxine have been determined of both UV-absorption and fluorescence spectroscopy. The binding Constants values measured at 293k are 1.659×10³ M^-1 for propylthiouracil and 1.013×10⁴ M^-1 for L-Thyroxine. The constant values of the Stern–Volmer quenching were determined to be 2.144×10³ L mol^-1 for propylthiouracil and 1.937×10³ L mol^-1 L-for Thyroxine. The UV-absorption intensity of HSA- hormones complexes has increased with increasing of propylthiouracil and L-Thyroxine concentration. With the rise in propylthiouracil and L-thyroxine concentrations, the fluorescence results indicate a decrease in HSA- hormone emission intensity. To determine the effects of protein secondary structure and hormone binding mechanisms, we have used FTIR spectroscopy with Fourier self-deconvolution technique and second derivative resolution enhancement, as well as curve-fitting methods for the investigation of the amide I, II, and III regions. The peak positions within the three amide regions (amide I, amide II and amide III) were allocated and any results were explored due to changes in concentration. Due to variations in hormone concentrations, the measurements of the FTIR spectra indicate a difference in the intensity of absorption bands.. FTIR Spectra measurements reflect a difference in the strength of the absorption bands due to changes in hormone concentrations.

Published in	European Journal of Biophysics (Volume 11, Issue 1)
DOI	10.11648/j.ejb.20231101.11
Page(s)	1-16
Creative Commons	This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright	Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

Thyroid Hormones (Propylthiouracil and L-Thyroxine), Human Serum Albumin, Binding Constant, Fourier Transform IR, UV/Visible Fluorescence Spectroscopy

References

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APA Style

Israa Ismail Abu Katteh, Husain Rashad Alsamamra, Musa Mahmoud Abu Teir. (2023). Studies of Thyroid Hormones (Propylthiouracil and L-Thyroxine) Interaction with Human Serum Albumin-Spectroscopic Approach. European Journal of Biophysics, 11(1), 1-16. https://doi.org/10.11648/j.ejb.20231101.11

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ACS Style

Israa Ismail Abu Katteh; Husain Rashad Alsamamra; Musa Mahmoud Abu Teir. Studies of Thyroid Hormones (Propylthiouracil and L-Thyroxine) Interaction with Human Serum Albumin-Spectroscopic Approach. Eur. J. Biophys. 2023, 11(1), 1-16. doi: 10.11648/j.ejb.20231101.11

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AMA Style

Israa Ismail Abu Katteh, Husain Rashad Alsamamra, Musa Mahmoud Abu Teir. Studies of Thyroid Hormones (Propylthiouracil and L-Thyroxine) Interaction with Human Serum Albumin-Spectroscopic Approach. Eur J Biophys. 2023;11(1):1-16. doi: 10.11648/j.ejb.20231101.11

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@article{10.11648/j.ejb.20231101.11,
  author = {Israa Ismail Abu Katteh and Husain Rashad Alsamamra and Musa Mahmoud Abu Teir},
  title = {Studies of Thyroid Hormones (Propylthiouracil and L-Thyroxine) Interaction with Human Serum Albumin-Spectroscopic Approach},
  journal = {European Journal of Biophysics},
  volume = {11},
  number = {1},
  pages = {1-16},
  doi = {10.11648/j.ejb.20231101.11},
  url = {https://doi.org/10.11648/j.ejb.20231101.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ejb.20231101.11},
  abstract = {In this work, UV-absorption, fluorescence spectroscopy and Fourier transform infrared (FTIR) spectroscopy were used to investigate the relationship between Propylthiouracil and L-Thyroxine with human serum albumin. The binding constants of propylthiouracil and L-Thyroxine have been determined of both UV-absorption and fluorescence spectroscopy. The binding Constants values measured at 293k are 1.659×103 M-1 for propylthiouracil and 1.013×104 M-1 for L-Thyroxine. The constant values of the Stern–Volmer quenching were determined to be 2.144×103 L mol-1 for propylthiouracil and 1.937×103 L mol-1 L-for Thyroxine. The UV-absorption intensity of HSA- hormones complexes has increased with increasing of propylthiouracil and L-Thyroxine concentration. With the rise in propylthiouracil and L-thyroxine concentrations, the fluorescence results indicate a decrease in HSA- hormone emission intensity. To determine the effects of protein secondary structure and hormone binding mechanisms, we have used FTIR spectroscopy with Fourier self-deconvolution technique and second derivative resolution enhancement, as well as curve-fitting methods for the investigation of the amide I, II, and III regions. The peak positions within the three amide regions (amide I, amide II and amide III) were allocated and any results were explored due to changes in concentration. Due to variations in hormone concentrations, the measurements of the FTIR spectra indicate a difference in the intensity of absorption bands.. FTIR Spectra measurements reflect a difference in the strength of the absorption bands due to changes in hormone concentrations.},
 year = {2023}
}

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TY  - JOUR
T1  - Studies of Thyroid Hormones (Propylthiouracil and L-Thyroxine) Interaction with Human Serum Albumin-Spectroscopic Approach
AU  - Israa Ismail Abu Katteh
AU  - Husain Rashad Alsamamra
AU  - Musa Mahmoud Abu Teir
Y1  - 2023/03/31
PY  - 2023
N1  - https://doi.org/10.11648/j.ejb.20231101.11
DO  - 10.11648/j.ejb.20231101.11
T2  - European Journal of Biophysics
JF  - European Journal of Biophysics
JO  - European Journal of Biophysics
SP  - 1
EP  - 16
PB  - Science Publishing Group
SN  - 2329-1737
UR  - https://doi.org/10.11648/j.ejb.20231101.11
AB  - In this work, UV-absorption, fluorescence spectroscopy and Fourier transform infrared (FTIR) spectroscopy were used to investigate the relationship between Propylthiouracil and L-Thyroxine with human serum albumin. The binding constants of propylthiouracil and L-Thyroxine have been determined of both UV-absorption and fluorescence spectroscopy. The binding Constants values measured at 293k are 1.659×103 M-1 for propylthiouracil and 1.013×104 M-1 for L-Thyroxine. The constant values of the Stern–Volmer quenching were determined to be 2.144×103 L mol-1 for propylthiouracil and 1.937×103 L mol-1 L-for Thyroxine. The UV-absorption intensity of HSA- hormones complexes has increased with increasing of propylthiouracil and L-Thyroxine concentration. With the rise in propylthiouracil and L-thyroxine concentrations, the fluorescence results indicate a decrease in HSA- hormone emission intensity. To determine the effects of protein secondary structure and hormone binding mechanisms, we have used FTIR spectroscopy with Fourier self-deconvolution technique and second derivative resolution enhancement, as well as curve-fitting methods for the investigation of the amide I, II, and III regions. The peak positions within the three amide regions (amide I, amide II and amide III) were allocated and any results were explored due to changes in concentration. Due to variations in hormone concentrations, the measurements of the FTIR spectra indicate a difference in the intensity of absorption bands.. FTIR Spectra measurements reflect a difference in the strength of the absorption bands due to changes in hormone concentrations.
VL  - 11
IS  - 1
ER  -

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Author Information

Israa Ismail Abu Katteh

Physics Department, Faculty of Science, Al-Quds University, Jerusalem, Palestine
Husain Rashad Alsamamra

Physics Department, Faculty of Science, Al-Quds University, Jerusalem, Palestine
Musa Mahmoud Abu Teir

Physics Department, Faculty of Science, Al-Quds University, Jerusalem, Palestine

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Israa Ismail Abu Katteh, Husain Rashad Alsamamra, Musa Mahmoud Abu Teir. (2023). Studies of Thyroid Hormones (Propylthiouracil and L-Thyroxine) Interaction with Human Serum Albumin-Spectroscopic Approach. European Journal of Biophysics, 11(1), 1-16. https://doi.org/10.11648/j.ejb.20231101.11

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ACS Style

Israa Ismail Abu Katteh; Husain Rashad Alsamamra; Musa Mahmoud Abu Teir. Studies of Thyroid Hormones (Propylthiouracil and L-Thyroxine) Interaction with Human Serum Albumin-Spectroscopic Approach. Eur. J. Biophys. 2023, 11(1), 1-16. doi: 10.11648/j.ejb.20231101.11

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AMA Style

Israa Ismail Abu Katteh, Husain Rashad Alsamamra, Musa Mahmoud Abu Teir. Studies of Thyroid Hormones (Propylthiouracil and L-Thyroxine) Interaction with Human Serum Albumin-Spectroscopic Approach. Eur J Biophys. 2023;11(1):1-16. doi: 10.11648/j.ejb.20231101.11

Copy | Download

@article{10.11648/j.ejb.20231101.11,
  author = {Israa Ismail Abu Katteh and Husain Rashad Alsamamra and Musa Mahmoud Abu Teir},
  title = {Studies of Thyroid Hormones (Propylthiouracil and L-Thyroxine) Interaction with Human Serum Albumin-Spectroscopic Approach},
  journal = {European Journal of Biophysics},
  volume = {11},
  number = {1},
  pages = {1-16},
  doi = {10.11648/j.ejb.20231101.11},
  url = {https://doi.org/10.11648/j.ejb.20231101.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ejb.20231101.11},
  abstract = {In this work, UV-absorption, fluorescence spectroscopy and Fourier transform infrared (FTIR) spectroscopy were used to investigate the relationship between Propylthiouracil and L-Thyroxine with human serum albumin. The binding constants of propylthiouracil and L-Thyroxine have been determined of both UV-absorption and fluorescence spectroscopy. The binding Constants values measured at 293k are 1.659×103 M-1 for propylthiouracil and 1.013×104 M-1 for L-Thyroxine. The constant values of the Stern–Volmer quenching were determined to be 2.144×103 L mol-1 for propylthiouracil and 1.937×103 L mol-1 L-for Thyroxine. The UV-absorption intensity of HSA- hormones complexes has increased with increasing of propylthiouracil and L-Thyroxine concentration. With the rise in propylthiouracil and L-thyroxine concentrations, the fluorescence results indicate a decrease in HSA- hormone emission intensity. To determine the effects of protein secondary structure and hormone binding mechanisms, we have used FTIR spectroscopy with Fourier self-deconvolution technique and second derivative resolution enhancement, as well as curve-fitting methods for the investigation of the amide I, II, and III regions. The peak positions within the three amide regions (amide I, amide II and amide III) were allocated and any results were explored due to changes in concentration. Due to variations in hormone concentrations, the measurements of the FTIR spectra indicate a difference in the intensity of absorption bands.. FTIR Spectra measurements reflect a difference in the strength of the absorption bands due to changes in hormone concentrations.},
 year = {2023}
}

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TY  - JOUR
T1  - Studies of Thyroid Hormones (Propylthiouracil and L-Thyroxine) Interaction with Human Serum Albumin-Spectroscopic Approach
AU  - Israa Ismail Abu Katteh
AU  - Husain Rashad Alsamamra
AU  - Musa Mahmoud Abu Teir
Y1  - 2023/03/31
PY  - 2023
N1  - https://doi.org/10.11648/j.ejb.20231101.11
DO  - 10.11648/j.ejb.20231101.11
T2  - European Journal of Biophysics
JF  - European Journal of Biophysics
JO  - European Journal of Biophysics
SP  - 1
EP  - 16
PB  - Science Publishing Group
SN  - 2329-1737
UR  - https://doi.org/10.11648/j.ejb.20231101.11
AB  - In this work, UV-absorption, fluorescence spectroscopy and Fourier transform infrared (FTIR) spectroscopy were used to investigate the relationship between Propylthiouracil and L-Thyroxine with human serum albumin. The binding constants of propylthiouracil and L-Thyroxine have been determined of both UV-absorption and fluorescence spectroscopy. The binding Constants values measured at 293k are 1.659×103 M-1 for propylthiouracil and 1.013×104 M-1 for L-Thyroxine. The constant values of the Stern–Volmer quenching were determined to be 2.144×103 L mol-1 for propylthiouracil and 1.937×103 L mol-1 L-for Thyroxine. The UV-absorption intensity of HSA- hormones complexes has increased with increasing of propylthiouracil and L-Thyroxine concentration. With the rise in propylthiouracil and L-thyroxine concentrations, the fluorescence results indicate a decrease in HSA- hormone emission intensity. To determine the effects of protein secondary structure and hormone binding mechanisms, we have used FTIR spectroscopy with Fourier self-deconvolution technique and second derivative resolution enhancement, as well as curve-fitting methods for the investigation of the amide I, II, and III regions. The peak positions within the three amide regions (amide I, amide II and amide III) were allocated and any results were explored due to changes in concentration. Due to variations in hormone concentrations, the measurements of the FTIR spectra indicate a difference in the intensity of absorption bands.. FTIR Spectra measurements reflect a difference in the strength of the absorption bands due to changes in hormone concentrations.
VL  - 11
IS  - 1
ER  -

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