Effects of Extremely Low Frequency Magnetic Field on the Secondary Structures of β-Amyloid and Human Serum Albumin

Saqer Mohamad Darwish; Husain Rashad Alsamamra; Sawsan Eid Abusharkh; Imtiaz Mohammed Khalid; Rania Abdeljalil Alfaqeh; Musa Mahmoud Abuteir

doi:doi:10.11648/j.ejb.20170506.11

Effects of Extremely Low Frequency Magnetic Field on the Secondary Structures of β-Amyloid and Human Serum Albumin

Saqer Mohamad Darwish, Husain Rashad Alsamamra, Sawsan Eid Abusharkh, Imtiaz Mohammed Khalid, Rania Abdeljalil Alfaqeh, Musa Mahmoud Abuteir

Published in European Journal of Biophysics (Volume 5, Issue 6)

Received: 28 November 2017 Accepted: 12 December 2017 Published: 10 January 2018

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Abstract

Human serum albumin and β-amyloid were exposed to extremely low frequency (ELF) magnetic field of 1.5 mT intensity and 50 Hz frequency. The effects of exposure were investigated in the mid-infrared region by means of Fourier self-deconvolution spectroscopic analysis. The experimental results suggest that exposure to the ELF magnetic field has reversible effects on the out of phase combination of N–H in plane bending and C–N stretching vibrations of the secondary structures of the two proteins. The exposure of β-amyloid and human serum albumin to ELF magnetic field affected the absorption spectra of the vibration bands by changes in peak positions for the amide II bands and changes of intensities in most of the bands in the amide I and amide II regions. In the fingerprint region, the most sensitive vibrations to the magnetic field are found to be in the (720-600) cm^-I range. After removing the magnetic field, it took the vibration bands more than 10 minutes of a gradual change toward returning to their original spectra, obtained before the exposure. It is suggested that hydrogen bonds can alter the frequency of a stretching vibration depending on the increase or decrease of strain on the vibrations.

Published in	European Journal of Biophysics (Volume 5, Issue 6)
DOI	10.11648/j.ejb.20170506.11
Page(s)	89-103
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), 2018. Published by Science Publishing Group

Keywords

FTIR-Spectroscopy, ELF-Magnetic Field, β-Amyloid, HAS, Protein Dynamics

References

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APA Style

Saqer Mohamad Darwish, Husain Rashad Alsamamra, Sawsan Eid Abusharkh, Imtiaz Mohammed Khalid, Rania Abdeljalil Alfaqeh, et al. (2018). Effects of Extremely Low Frequency Magnetic Field on the Secondary Structures of β-Amyloid and Human Serum Albumin. European Journal of Biophysics, 5(6), 89-103. https://doi.org/10.11648/j.ejb.20170506.11

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ACS Style

Saqer Mohamad Darwish; Husain Rashad Alsamamra; Sawsan Eid Abusharkh; Imtiaz Mohammed Khalid; Rania Abdeljalil Alfaqeh, et al. Effects of Extremely Low Frequency Magnetic Field on the Secondary Structures of β-Amyloid and Human Serum Albumin. Eur. J. Biophys. 2018, 5(6), 89-103. doi: 10.11648/j.ejb.20170506.11

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AMA Style

Saqer Mohamad Darwish, Husain Rashad Alsamamra, Sawsan Eid Abusharkh, Imtiaz Mohammed Khalid, Rania Abdeljalil Alfaqeh, et al. Effects of Extremely Low Frequency Magnetic Field on the Secondary Structures of β-Amyloid and Human Serum Albumin. Eur J Biophys. 2018;5(6):89-103. doi: 10.11648/j.ejb.20170506.11

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@article{10.11648/j.ejb.20170506.11,
  author = {Saqer Mohamad Darwish and Husain Rashad Alsamamra and Sawsan Eid Abusharkh and Imtiaz Mohammed Khalid and Rania Abdeljalil Alfaqeh and Musa Mahmoud Abuteir},
  title = {Effects of Extremely Low Frequency Magnetic Field on the Secondary Structures of β-Amyloid and Human Serum Albumin},
  journal = {European Journal of Biophysics},
  volume = {5},
  number = {6},
  pages = {89-103},
  doi = {10.11648/j.ejb.20170506.11},
  url = {https://doi.org/10.11648/j.ejb.20170506.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ejb.20170506.11},
  abstract = {Human serum albumin and β-amyloid were exposed to extremely low frequency (ELF) magnetic field of 1.5 mT intensity and 50 Hz frequency. The effects of exposure were investigated in the mid-infrared region by means of Fourier self-deconvolution spectroscopic analysis. The experimental results suggest that exposure to the ELF magnetic field has reversible effects on the out of phase combination of N–H in plane bending and C–N stretching vibrations of the secondary structures of the two proteins. The exposure of β-amyloid and human serum albumin to ELF magnetic field affected the absorption spectra of the vibration bands by changes in peak positions for the amide II bands and changes of intensities in most of the bands in the amide I and amide II regions. In the fingerprint region, the most sensitive vibrations to the magnetic field are found to be in the (720-600) cm-I range. After removing the magnetic field, it took the vibration bands more than 10 minutes of a gradual change toward returning to their original spectra, obtained before the exposure. It is suggested that hydrogen bonds can alter the frequency of a stretching vibration depending on the increase or decrease of strain on the vibrations.},
 year = {2018}
}

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TY  - JOUR
T1  - Effects of Extremely Low Frequency Magnetic Field on the Secondary Structures of β-Amyloid and Human Serum Albumin
AU  - Saqer Mohamad Darwish
AU  - Husain Rashad Alsamamra
AU  - Sawsan Eid Abusharkh
AU  - Imtiaz Mohammed Khalid
AU  - Rania Abdeljalil Alfaqeh
AU  - Musa Mahmoud Abuteir
Y1  - 2018/01/10
PY  - 2018
N1  - https://doi.org/10.11648/j.ejb.20170506.11
DO  - 10.11648/j.ejb.20170506.11
T2  - European Journal of Biophysics
JF  - European Journal of Biophysics
JO  - European Journal of Biophysics
SP  - 89
EP  - 103
PB  - Science Publishing Group
SN  - 2329-1737
UR  - https://doi.org/10.11648/j.ejb.20170506.11
AB  - Human serum albumin and β-amyloid were exposed to extremely low frequency (ELF) magnetic field of 1.5 mT intensity and 50 Hz frequency. The effects of exposure were investigated in the mid-infrared region by means of Fourier self-deconvolution spectroscopic analysis. The experimental results suggest that exposure to the ELF magnetic field has reversible effects on the out of phase combination of N–H in plane bending and C–N stretching vibrations of the secondary structures of the two proteins. The exposure of β-amyloid and human serum albumin to ELF magnetic field affected the absorption spectra of the vibration bands by changes in peak positions for the amide II bands and changes of intensities in most of the bands in the amide I and amide II regions. In the fingerprint region, the most sensitive vibrations to the magnetic field are found to be in the (720-600) cm-I range. After removing the magnetic field, it took the vibration bands more than 10 minutes of a gradual change toward returning to their original spectra, obtained before the exposure. It is suggested that hydrogen bonds can alter the frequency of a stretching vibration depending on the increase or decrease of strain on the vibrations.
VL  - 5
IS  - 6
ER  -

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Author Information

Saqer Mohamad Darwish

Physics Department, Al-Quds University, Abu-Dies, Jerusalem, Palestine
Husain Rashad Alsamamra

Physics Department, Al-Quds University, Abu-Dies, Jerusalem, Palestine
Sawsan Eid Abusharkh

Physics Department, Al-Quds University, Abu-Dies, Jerusalem, Palestine
Imtiaz Mohammed Khalid

Chemistry Department, Birzeit University, Birzeit, Palestine
Rania Abdeljalil Alfaqeh

Physics Department, Al-Quds University, Abu-Dies, Jerusalem, Palestine
Musa Mahmoud Abuteir

Physics Department, Al-Quds University, Abu-Dies, Jerusalem, Palestine

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Saqer Mohamad Darwish, Husain Rashad Alsamamra, Sawsan Eid Abusharkh, Imtiaz Mohammed Khalid, Rania Abdeljalil Alfaqeh, et al. (2018). Effects of Extremely Low Frequency Magnetic Field on the Secondary Structures of β-Amyloid and Human Serum Albumin. European Journal of Biophysics, 5(6), 89-103. https://doi.org/10.11648/j.ejb.20170506.11

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ACS Style

Saqer Mohamad Darwish; Husain Rashad Alsamamra; Sawsan Eid Abusharkh; Imtiaz Mohammed Khalid; Rania Abdeljalil Alfaqeh, et al. Effects of Extremely Low Frequency Magnetic Field on the Secondary Structures of β-Amyloid and Human Serum Albumin. Eur. J. Biophys. 2018, 5(6), 89-103. doi: 10.11648/j.ejb.20170506.11

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AMA Style

Saqer Mohamad Darwish, Husain Rashad Alsamamra, Sawsan Eid Abusharkh, Imtiaz Mohammed Khalid, Rania Abdeljalil Alfaqeh, et al. Effects of Extremely Low Frequency Magnetic Field on the Secondary Structures of β-Amyloid and Human Serum Albumin. Eur J Biophys. 2018;5(6):89-103. doi: 10.11648/j.ejb.20170506.11

Copy | Download

@article{10.11648/j.ejb.20170506.11,
  author = {Saqer Mohamad Darwish and Husain Rashad Alsamamra and Sawsan Eid Abusharkh and Imtiaz Mohammed Khalid and Rania Abdeljalil Alfaqeh and Musa Mahmoud Abuteir},
  title = {Effects of Extremely Low Frequency Magnetic Field on the Secondary Structures of β-Amyloid and Human Serum Albumin},
  journal = {European Journal of Biophysics},
  volume = {5},
  number = {6},
  pages = {89-103},
  doi = {10.11648/j.ejb.20170506.11},
  url = {https://doi.org/10.11648/j.ejb.20170506.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ejb.20170506.11},
  abstract = {Human serum albumin and β-amyloid were exposed to extremely low frequency (ELF) magnetic field of 1.5 mT intensity and 50 Hz frequency. The effects of exposure were investigated in the mid-infrared region by means of Fourier self-deconvolution spectroscopic analysis. The experimental results suggest that exposure to the ELF magnetic field has reversible effects on the out of phase combination of N–H in plane bending and C–N stretching vibrations of the secondary structures of the two proteins. The exposure of β-amyloid and human serum albumin to ELF magnetic field affected the absorption spectra of the vibration bands by changes in peak positions for the amide II bands and changes of intensities in most of the bands in the amide I and amide II regions. In the fingerprint region, the most sensitive vibrations to the magnetic field are found to be in the (720-600) cm-I range. After removing the magnetic field, it took the vibration bands more than 10 minutes of a gradual change toward returning to their original spectra, obtained before the exposure. It is suggested that hydrogen bonds can alter the frequency of a stretching vibration depending on the increase or decrease of strain on the vibrations.},
 year = {2018}
}

Copy | Download

TY  - JOUR
T1  - Effects of Extremely Low Frequency Magnetic Field on the Secondary Structures of β-Amyloid and Human Serum Albumin
AU  - Saqer Mohamad Darwish
AU  - Husain Rashad Alsamamra
AU  - Sawsan Eid Abusharkh
AU  - Imtiaz Mohammed Khalid
AU  - Rania Abdeljalil Alfaqeh
AU  - Musa Mahmoud Abuteir
Y1  - 2018/01/10
PY  - 2018
N1  - https://doi.org/10.11648/j.ejb.20170506.11
DO  - 10.11648/j.ejb.20170506.11
T2  - European Journal of Biophysics
JF  - European Journal of Biophysics
JO  - European Journal of Biophysics
SP  - 89
EP  - 103
PB  - Science Publishing Group
SN  - 2329-1737
UR  - https://doi.org/10.11648/j.ejb.20170506.11
AB  - Human serum albumin and β-amyloid were exposed to extremely low frequency (ELF) magnetic field of 1.5 mT intensity and 50 Hz frequency. The effects of exposure were investigated in the mid-infrared region by means of Fourier self-deconvolution spectroscopic analysis. The experimental results suggest that exposure to the ELF magnetic field has reversible effects on the out of phase combination of N–H in plane bending and C–N stretching vibrations of the secondary structures of the two proteins. The exposure of β-amyloid and human serum albumin to ELF magnetic field affected the absorption spectra of the vibration bands by changes in peak positions for the amide II bands and changes of intensities in most of the bands in the amide I and amide II regions. In the fingerprint region, the most sensitive vibrations to the magnetic field are found to be in the (720-600) cm-I range. After removing the magnetic field, it took the vibration bands more than 10 minutes of a gradual change toward returning to their original spectra, obtained before the exposure. It is suggested that hydrogen bonds can alter the frequency of a stretching vibration depending on the increase or decrease of strain on the vibrations.
VL  - 5
IS  - 6
ER  -

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