Volume 5, Issue 6, December 2017, Page: 89-103
Effects of Extremely Low Frequency Magnetic Field on the Secondary Structures of β-Amyloid and Human Serum Albumin
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
Received: Nov. 28, 2017;       Accepted: Dec. 12, 2017;       Published: Jan. 10, 2018
DOI: 10.11648/j.ejb.20170506.11      View  1257      Downloads  68
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.
Keywords
FTIR-Spectroscopy, ELF-Magnetic Field, β-Amyloid, HAS, Protein Dynamics
To cite this article
Saqer Mohamad Darwish, Husain Rashad Alsamamra, Sawsan Eid Abusharkh, Imtiaz Mohammed Khalid, Rania Abdeljalil Alfaqeh, Musa Mahmoud Abuteir, Effects of Extremely Low Frequency Magnetic Field on the Secondary Structures of β-Amyloid and Human Serum Albumin, European Journal of Biophysics. Vol. 5, No. 6, 2017, pp. 89-103. doi: 10.11648/j.ejb.20170506.11
Copyright
Copyright © 2017 Authors retain the copyright of this article.
This article is an open access article distributed under the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Reference
[1]
A. Elliot and E. J. Ambrose, “Structure of Synthetic Polypeptides," Nature, 165, (1950) 921-922.
[2]
T. Miyazawa, ‘Infrared Spectra and Helical Conformations’, in “Poly-a- amino Acids,” ed. G. D. Fasman, Marcel Dekker, New York, (1967) 69–103.
[3]
S. Krimm and J. Bandekar, “Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins,” Adv. Protein Chem., 38, (1986) 181-364.
[4]
Byler DM, Susi H., “Examination of the secondary structure of proteins by deconvolved FTIR spectra,” Biopolymer, 25 (1986) 469−487.
[5]
Surewicz, W. K., Mantsch, H. H. and Chapman, D., “Determination of Protein Secondary Structure by Fourier Transform Infrared Spectroscopy: A Critical Assessment,” Biochemistry, 32 (1993) 389-394.
[6]
M. X. Xie, Y. Liu, “Studies on amide III infrared bands for the secondary structure determination of proteins,” Chem. J. Chin. Univ.—Chinese 24 (2003) 226–231.
[7]
S. Cai, B. R. Singh, “Identification of ß-turn and random coil amide III infrared bands for secondary structure estimation of proteins,” Biophys. Chem. 80 (1999) 7–20.
[8]
S. Cai, B. R. Singh, “A distinct utility of the amide III infrared band for secondary structure estimation of aqueous protein solutions using partial least squares methods,” Biochemistry 43 (2004) 2541–2549.
[9]
R. J. Ellis and F. U. Hartl, “Principles of protein folding in the cellular environment,” Current Opinion in Structural Biology, vol. 9, no. 1 (1999) 102–110.
[10]
M. J. Gething and J. Sambrook, “Protein folding in the cell,” Nature, vol. 355, no. 6355 (1992) 33–45.
[11]
Stroud, J. C., Liu, C., Teng, P. K. and Eisenberg, D. (2012) Toxic Fibrillar Oligomers of Amyloid-β Have Cross-βStructure. Proceedings of the National Academy of Sciences of the United States of America, 109, 7717-7722.
[12]
Lu, M., Hiramatsu, H., Goto, Y. and Kitagawa, T., “Structure of Interacting Segments in the Growing Amyloid Fibril of β2-Microglobulin Probed with IR Spectroscopy,” Journal of Molecular Biology, 362 (2006) 355-364.
[13]
Saqer M. Darwish, Shurook Y. Aiaidah, Imtiaz M. Khalid, Musa M. Abuteir, Lena Qawasmi, “Spectroscopic Investigations of β-Amyloid Interactions with Propofol and L-Arginine,” Open Journal of Biophysics, 2015, 5,(2015) 50-67.
[14]
T. Peters, “Structure of serum albumin,”Adv. Protein Chem. 37 (1985) 161-245.
[15]
Santoro N, Lisi A, Pozzi D, Pasquali E, Serafino A, GrimaldiS.,“Effect of extremely low frequency (ELF) magnetic field exposure on morphological and biophysical properties of human lymphoid cell line (Raji),” Biochim. Biophys. Acta, 1357 (1997) 281–290.
[16]
Toshitaka Ikehara, Hisao Yamaguchi, Keiko Hosokawa, Hiroshi Miyamoto, Katsuo Aizawa, “Effects of ELF magnetic field on membrane protein structure of living Hela cells studied by Fourier transform infrared spectroscopy,” Bioelectromagnetics 24 (2003) 457-464.
[17]
WHO, “Extremely low frequency (ELF) fields,” Environmental Health Criteria 35, World Health Organization, Geneva, Switzerland, 1984.
[18]
Emanuele Calabro and Salvatore Magazu, “Electromagnetic Fields Effects on the Secondary Structure of Lysozyme and Bioprotective Effectiveness of Trehalose,” Advances in Physical Chemistry, 2012 (2012) 1-6.
[19]
S. Magazu, E. Calabro, and S. Campo, “FTIR spectroscopy studies on the bioprotective effectiveness of trehalose on human hemoglobin aqueous solutions under 50 Hz electromagnetic field exposure,” J. Physical Chemistry B, 114, no. 37 (2010) 12144–12149.
[20]
Mehmet Zulkuf Akdag, Suleyman Dasdag, Dilek Ulker Cakir, Beran Yokus, Goksel Kizil & Murat Kizil, Do 100- and 500-mT ELF magnetic fields alter beta-amyloid protein, protein carbonyl and malondialdehyde in rat brains?, Electromagnetic Biology and Medicine, 32, 3 (2013) 363–372.
[21]
Marcella Reale, Mohammad A. Kamal, Antonia Patruno, Erica Costantini, Chiara D’ Angelo, Miko Pesce, Nigel H. Greig, Neuronal Cellular Responses to Extremely Low Frequency Electromagnetic Field Exposure: Implications Regarding Oxidative Stress and Neurodegeneration, PLOS One, 9, 8 (2014) doi: 10.1371.
[22]
Greenland S, Sheppard AR, Kaune WT, Poole C, Kelsh MA. 2000. A pooled analysis of magnetic fields, wire codes, and childhood leukemia. Epidemiology 11, 624–634.
[23]
Ahlbom A, et al. 2000. A pooled analysis of magnetic fields and childhood leukaemia. Br. J. Cancer 83, 692–698.
[24]
International Agency for Research on Cancer 2002. Static and extremely low-frequency (ELF) electric and magnetic fields. IARC monographs on the evaluation of carcinogenic risks to humans, vol. 80 Lyon, France: IARC.
[25]
National Radiological Protection Board 2001. ELF electromagnetic fields and the risk of cancer. Report of an Advisory Group on Non-ionising Radiation. Documents of the NRPB, vol 12 Chilton, Oxon, UK: NRPB.
[26]
Liedvogel M, Mouritsen H. 2010. Cryptochromes: a potential magnetoreceptor: what do we know and what do we want to know? J. R. Soc. Interface 7, S147–S162.
[27]
Ritz T, Adem S, Schulten K., “A model for photoreceptor-based magnetoreception in birds,” Biophys. J. 78 (2000) 707–718.
[28]
Shubhajit Paul, Alexey S. Kiryutin, Jinping Guo, Konstantin L. Ivanov, Jörg Matysik, Alexandra V. Yurkovskaya & Xiaojie Wang, Magnetic field effect in natural cryptochrome explored with model compound, Scientific Reports 7: 11892 | DOI: 10.1038/s41598-017-10356-4 (2017).
[29]
Yong E., "Flying sly: supersensory perception," New Sci. 2788 (2010) 42– 45.
[30]
Ball P.," Physics of life: the dawn of quantum biology," Nature 474 (2011) 272– 274.
[31]
Hoff AJ.," Magnetic field effects on photosynthetic reactions," Q. Rev. Biophys. 14 (1981) 599–665.
[32]
Van Dijk B, Carpenter JKH, Hoff AJ, Hore PJ.," Magnetic field effects on the recombination kinetics of radical pairs," J. Phys. Chem. B 102 (1988) 464–472.
[33]
Liu Y, Edge R, Henbest K, Timmel CR, Hore PJ, GastP.,"Magnetic field effect on singlet oxygen production in a biochemical system," Chem. Commun. 2 (2005) 174–176.
[34]
Alex R. Jones, magnetic field effects in proteins, Molucular Physics. 14, 11 (2016) 1691-1702.
[35]
Emrys W. Evans, Charlotte A. Dodson, Kiminori Maeda, Till Biskup, C. J. Wedge, Christiane R. Timmel, Magnetic field effect on flavoproteins and related systems, Interface Focus, 3 (5) 2013: 20130037. doi: 10.1098/rsfs.2013.0037.
[36]
Saqer M. Darwish, Sawsan E. Abu sharkh, Musa M. Abu Teir, Sami A. Makharza, Mahmoud M. Abu-hadid," Spectroscopic investigations of pentobarbital interaction with human serum albumin," Journal of Molecular Structure 963 (2010) 122–129.
[37]
R. K. Dukor, J. M. Chalmers, P. R. Griffiths (Eds.), Vibrational Spectroscopy in the Detection of Cancer, Handbook of Vibrational Spectroscopy, vol. 5, Wiley, Chichester, 2001 (Chapter 3).
[38]
Sirotkin, V. A., Zinatullin, A. N., Solomonov, B. N., Faizullin, D. A. and Fedotov, V. D.," Calorimetric and Fourier transform Infrared Spectroscopic Study of Solid Proteins Immersed in Low Water Organic Solvents," Biochimicaet Biophysica Acta, 1547 (2001) 359-369.
[39]
Y. N. Chirgadze, O. V. Fedorov, N. P. Trushina," Secondary structure of Na+, K+-dependent adenosine triphosphatase," Biopolymers 14 (1975) 679-694.
[40]
Cerf, E., et al., "Antiparallel β-Sheet: A Signature Structure of the Oligomeric Amyloid β-Peptide," Biochemical Journal, 421 (2007) 415-423.
[41]
Sarroukh, R., Cerf, E., Derclaye, S., Dufrêne, Y. F., Goormaghtigh, E., Ruysschaert, J. M., Raussens, V., "Transformation of Amyloid β(1-40) Oligomers into Fibrils Is Characterized by a Major Change in Secondary Structure," Cell. Cellular and Molecular Life Sciences, 68 (2011) 1429-1438.
[42]
Dong A, Huang P, Caughey WS., "Redox-dependent changes in β-extended chain and turn structures of cytochrome c in water solution determined by second derivative amide I infrared spectra. Biochemistry," 31 (1992) 182-189.
[43]
Susi H, Byler DM.," Resolution-enhanced fourier transform infrared spectroscopy of enzymes," Methods Enzymol, 130 (1986) 290−311.
[44]
Kong, J. and Yu, S., "Fourier Transform Infrared Spectroscopic Analysis of Protein Secondary Structures,"Acta Biochimicaet Biophysica Sinica, 39 (2007) 549-559.
[45]
G. Deleris, C. Petibios, Vib. Spectrosc. 32 (2003) 129-136.
[46]
E. Bramanti, E. Benedetti, "Determination of the secondary structure of isomeric forms of human serum albumin by a particular frequency deconvolution procedure applied to Fourier transform IR analysis," Biopolymers 38 (1996) 639-653.
[47]
Emanuele Calabro and Salvatore Magazu, Unfolding-induced in Haemoglobin by Exposure to Electromagnetic Fields: A FTIR Spectroscopy Study, Orient. J. Chem., Vol. 30 (1), (2014) 31-35.
[48]
Heinz Fabian and Werner Mantele, "inferred spectroscopy of proteins, Biochemical applications", John Wiley &son’s ltd. 2002.
[49]
Patrick Garidel and Heidrun Schott, Fourier-Transform Midinfrared spectroscopy for analysis and screening of liquid protein formulations, Bioprocess international 40 (2006) 48-55.
[50]
H. Deng, R. Callender, "Raman spectroscopic studies of the structures, energetics, and bond distortions of substrates bound to enzymes," Methods Enzymol. 308 (1999) 176–201.
[51]
V Zablotskii, O Lunov, S Kubinova, T Polyakova, E Sykova and A Dejneka, Effects of high-gradient magnetic fields on living cell machinery, J. Phys. D: Appl. Phys. 49 (2016) 1-23.
[52]
Kubelka, T. A. Keiderling," The anomolous infrared amidei intensity distribution in 13C isotopically labelled peptide," J. Am. chem. soc. 123 (2001) 6142-6150.
[53]
Andreas Barth, "IR spectroscopy of proteins," Biochimicaet Biophysica Acta, 1767 (2007) 1073–1101.
[54]
N. P. Colthump, L. H, Daly, S. B. Wiberley, Introduction to Inferred and Raman Spectroscopy 2nd ed. Academic press. New York 1975.
[55]
H. Torri, T. Tatsumi," Effects of hydrogen on the structure vibrational wavenumbers, vibrational force field and resonance Raman intensities of N-methylacetamide," J. Raman spectroscopy, 29 (1998) 537-546.
[56]
B. Mennucci, J. M. Martinez," How to model solavation of piptides? Insights from quantum Mechanical and molecular dynamics study of N-methylacetamide I," J. phys. chem. 109 (2005) 9818-9829.
[57]
P. Huang, A. Dong, and W. S. Caughey, “Effects of dimethyl sulfoxide, glycerol, and ethylene glycol on secondary structures of cytochrome c and lysozyme as observed by infrared spectroscopy,” Journal of Pharmaceutical Sciences, 84, no. 4 (1995) 387–392.
[58]
R. Bauer, R. Carrotta, C. Rischel, and L. Øgendal, “Characterization and isolation of intermediates in β-lactoglobulin heat aggregation at high pH,” Biophysical Journal, vol. 79, no. 2 (2000) 1030–1038.
[59]
S. Magazu, E. Calabro, and S. Campo, “Studying the electromagnetic-induced changes of the secondary structure of bovine serum albumin and the bioprotective effectiveness of trehalose by FTIR spectroscopy,” Journal of Physical Chemistry B, vol. 115, no. 21 (2011) 6818–6826.
[60]
Yu. N. Chirgadze, N. A. Nevskaya Infrared spectra and resonance interaction of amide-I vibration of the antiparallel-chain pleated sheet, biopolymer, Volume 15, Issue 4 (1976) 607–625.
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