Spectroscopic Investigations of β-Amyloid Interactions with Propofol and L-Arginine
Author(s)
Saqer M. Darwish1*,
Shurook Y. Aiaidah1,
Imtiaz M. Khalid2,
Musa M. Abuteir1,
Lena Qawasmi3
Affiliation(s)
1 Physics Department, Al-Quds University, al-Bireh, Palestine. 2 University College for Educational Sciences. 3 Nano - Technology Center.
1 Physics Department, Al-Quds University, al-Bireh, Palestine. 2 University College for Educational Sciences. 3 Nano - Technology Center.
ABSTRACT
Beta amyloid (Aβ) aggregation has been characterized to be responsible for several amyloid diseases. Fourier transform infrared (FTIR) spectroscopy, fluorescence, and atomic force microscopy (AFM) are used to investigate induced changes in the secondary structure of Aβ upon thermal denaturation and interaction with propofol and L-arginine. Spectral analysis has revealed an effective static quenching for the intrinsic fluorescence of Aβ by propofol and l-arginine with binding constants of 2.81 × 102 M-1 for Aβ-propofol and 0.37 × 102 M-1 for Aβ-L-arginine. Fourier self-deconvolution (FSD) technique has been used to evaluate the relative intensity changes in the spectra of the component bands in the amide I and amide II regions at different ligand’s concentration in the protein complex. The analysis showed a decrease in the intensities of the parallel beta bands of propofol and L-arginine interactions with Aβ, accompanied with an increase in the antiparallel bands for the Aβ-propofol interaction and a decrease for the Aβ-l-arginine interaction. The relative increase in peaks’ intensities at 1694 cm-1 and 1531 cm-1 for the propofol interaction is linked to the formation of oligomers in the protein.
Beta amyloid (Aβ) aggregation has been characterized to be responsible for several amyloid diseases. Fourier transform infrared (FTIR) spectroscopy, fluorescence, and atomic force microscopy (AFM) are used to investigate induced changes in the secondary structure of Aβ upon thermal denaturation and interaction with propofol and L-arginine. Spectral analysis has revealed an effective static quenching for the intrinsic fluorescence of Aβ by propofol and l-arginine with binding constants of 2.81 × 102 M-1 for Aβ-propofol and 0.37 × 102 M-1 for Aβ-L-arginine. Fourier self-deconvolution (FSD) technique has been used to evaluate the relative intensity changes in the spectra of the component bands in the amide I and amide II regions at different ligand’s concentration in the protein complex. The analysis showed a decrease in the intensities of the parallel beta bands of propofol and L-arginine interactions with Aβ, accompanied with an increase in the antiparallel bands for the Aβ-propofol interaction and a decrease for the Aβ-l-arginine interaction. The relative increase in peaks’ intensities at 1694 cm-1 and 1531 cm-1 for the propofol interaction is linked to the formation of oligomers in the protein.
KEYWORDS
FTIR Spectroscopy, Oligomeric Aβ, Alzheimer’s Disease, Amyloid β-Peptide, Antiparallel β-Sheet
FTIR Spectroscopy, Oligomeric Aβ, Alzheimer’s Disease, Amyloid β-Peptide, Antiparallel β-Sheet
Cite this paper
Darwish, S. , Aiaidah, S. , Khalid, I. , Abuteir, M. and Qawasmi, L. (2015) Spectroscopic Investigations of β-Amyloid Interactions with Propofol and L-Arginine. Open Journal of Biophysics, 5, 50-67. doi: 10.4236/ojbiphy.2015.52005.
Darwish, S. , Aiaidah, S. , Khalid, I. , Abuteir, M. and Qawasmi, L. (2015) Spectroscopic Investigations of β-Amyloid Interactions with Propofol and L-Arginine. Open Journal of Biophysics, 5, 50-67. doi: 10.4236/ojbiphy.2015.52005.
References
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[1] Roher, A.E., Chaney, M.O., Kuo, Y.M., Webster, S.D., Stine, W.B., Haverkamp, L.J., Woods, A.S., Cotter, R,J., Tuohy, J.M., Krafft, G.A., Bonnell, B.S. and Emmerling, M.R. (1996) Morphology and Toxicity of Abeta-(1-42) Dimer Derived from Neuritic and Vascular Amyloid Deposits of Alzheimer’s Disease. The Journal of Biological Chemistry, 271, 20631-20635.
http://dx.doi.org/10.1074/jbc.271.34.20631 [2] Klein, W.I., Krafft, G.A. and Finch, C.E. (2001) Targeting Small Aβ Oligomers: The Solution to an Alzheimer’s Conundrum. Trends in Neurosciences, 24, 219-224.
http://dx.doi.org/10.1016/S0166-2236(00)01749-5 [3] Dahlgren, K.W., Manelli, A.M., Stine, W.B., Baker, L.K., Kraft, G.K. and LaDu, M.J. (2002) Oligomeric and Fibrillar Species of Amyloid-Beta Peptide Differentially Affect Neuronal Viability. The Journal of Biological Chemistry, 277, 32046-32053.
http://dx.doi.org/10.1074/jbc.M201750200 [4] Kayed, R., Head, E., Thompson, J.L., Mcintire, T.M., Milton, S.C., Cotman, C.W. and Glabe, C.G. (2003) Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis. Science, 300, 486-489.
http://dx.doi.org/10.1126/science.1079469 [5] Hsia, A.Y., et al. (1999) Plaque-Independent Disruption of Neural Circuits in Alzheimer’s Disease Mouse Models. Proceedings of the National Academy of Sciences of the United States of America, 96, 3228-3233.
http://dx.doi.org/10.1073/pnas.96.6.3228 [6] Chapman, P.F., et al. (1999) Impaired Synaptic Plasticity and Learning in Aged Amyloid Precursor Protein Transgenic Mice. Nature Neuroscience, 2, 271-276.
http://dx.doi.org/10.1038/6374 [7] Walsh, D.M., Klyubin, I., Fadeeva, J.V., Cullen, W.K., Anwyl, R., Wolfe, M.S., Rowan, M.J. and Selkoe, D.J. (2002) Naturally Secreted Oligomers of Amyloid β Protein Potently Inhibit Hippocampal Long-Term Potentiation in Vivo. Nature, 41, 535-539.
http://dx.doi.org/10.1038/416535a [8] Hardy, J. and Selkoe, D.J., (2002) The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics. Science, 297, 353-356.
http://dx.doi.org/10.1126/science.1072994 [9] Cerf, E., et al. (2007) Antiparallel β-Sheet: A Signature Structure of the Oligomeric Amyloid β-Peptide. Biochemical Journal, 421, 415-423.
http://dx.doi.org/10.1042/BJ20090379 [10] Carnini, A., Lear, J.D. and Eckenhoff, R.G. (2007) Inhaled Anesthetic Modulation of Amyloid Aβ1-40 Assembly and Growth. Current Alzheimer Research, 4, 233-241.
http://dx.doi.org/10.2174/156720507781077278 [11] Bohnen, N.I., Warner, M.A., Kokmen, E., Beard, C.M. and Kurland, L.T. (1994) Alzheimer-Disease and Cumulative Exposure to Anesthesia—A Case-Control Study. Journal of the American Geriatrics Society, 42, 198-201. [12] Muravchick, S. and Smith, D.S. (1995) Parkinsonian Symptoms during Emergence from General-Anesthesia. Anesthesiology, 82, 305-307.
http://dx.doi.org/10.1097/00000542-199501000-00039 [13] Surewicz, W.K., Mantsch, H.H. and Chapman, D. (1993) Determination of Protein Secondary Structure by Fourier Transform Infrared Spectroscopy: A Critical Assessment. Biochemistry, 32, 389-394.
http://dx.doi.org/10.1021/bi00053a001 [14] Stephanos, J.J. and Inorg, J. (1996) Drug-Protein Interactions. Two-Site Binding of Heterocylclic Ligands to a Monomeric Hemoglobin. Journal of Inorganic Biochemistry, 62, 155-169.
http://dx.doi.org/10.1016/0162-0134(95)00144-1 [15] Klotz, M.I. and Hunston, L.D. (1971) Properties of Graphical Representations of Multiple Classes of Binding Sites. Biochemistry, 10, 3065-3069.
http://dx.doi.org/10.1021/bi00792a013 [16] Klotz, M.I. (1982) Numbers of Receptor Sites from Scatchard Graphs: Facts and Fantasies. Science, 217, 1247-1249.
http://dx.doi.org/10.1126/science.6287580 [17] Bhattacharya, A.A., Gruene, T. and Curry, S. (2000) Crystallographic Analysis Reveals Common Modes of Binding of Medium and Long-Chain Fatty Acids to Human Serum Albumin. Journal of Molecular Biology, 303, 721-732.
http://dx.doi.org/10.1006/jmbi.2000.4158 [18] Purcell, M., Neault, J.F. and Tajmir-Riahi, H.A. (2000) Interaction of Taxol with Human Serum Albumin. Biochimica et Biophysica Acta, 1478, 61-68.
http://dx.doi.org/10.1016/S0167-4838(99)00251-4 [19] Sarroukh, R., Cerf, E., Derclaye, S., Dufrêne, Y.F., Goormaghtigh, E., Ruysschaert, J.-M. and Raussens, V. (2011) 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, 1429-1438.
http://dx.doi.org/10.1007/s00018-010-0529-x [20] Amaro, M., Kubiak-Ossowska, K., Birch, D.J.S. and Rolinski, O.J. (2013) Initial Stages of Beta-Amyloid Aβ1-40 and Aβ1-42 Oligomerization Observed Using Fluorescence Decay and Molecular Dynamics Analyses of Tyrosine. Methods and Applications in Fluorescence, 1, Article ID: 015006.
http://dx.doi.org/10.1088/2050-6120/1/1/015006 [21] Turro, N.J. (1991) Modern Molecular Photochemistry. University Science Books, Sausalito. [22] Jianghong, T., Ning, L., Xianghong, H. and Guohua, Z. (2008) Investigation of the Interaction between Sophoricoside and Human Serum Albumin by Optical Spectroscopy and Molecular Modeling Methods. Journal of Molecular Structure, 889, 408-414.
http://dx.doi.org/10.1016/j.molstruc.2008.02.031 [23] Li, J., Ren, C., Zhang, Y., Liu, X., Yao, X. and Hu, Z. (2008) Human Serum Albumin Interaction with Honokiol Studied Using Optical Spectroscopy and Molecular Modeling Methods. Journal of Molecular Structure, 881, 90-96.
http://dx.doi.org/10.1016/j.molstruc.2007.08.039 [24] Sheehan, D. (2009) Physical Biochemistry: Principles and Applications. 2nd Edition, John Wiley & Sons, Hoboken. [25] Tian, J.N., Liu, J.Q., Zhang, J.Y., Hu, Z.D. and Chen, X.G. (2003) Fluorescence Studies on the Interactions of Barbaloin with Bovine Serum Albumin. Chemical & Pharmaceutical Bulletin, 51, 579-582.
http://dx.doi.org/10.1248/cpb.51.579 [26] Lakowicz, J.R. (2006) Principles of Fluorescence Spectroscopy. 3rd Edition, Springer Science, New York. [27] Kong, J. and Yu, S. (2007) Fourier Transform Infrared Spectroscopic Analysis of Protein Secondary Structures. Acta Biochimica et Biophysica Sinica, 39, 549-559.
http://dx.doi.org/10.1111/j.1745-7270.2007.00320.x [28] Darwish, S.M., Ghithan, J., Abuteir, M.M., Faroun, M. and Abu-Hadid, M.M. (2013) Spectroscopic Investigation of Pentobarbital Interaction with Transthyretin. Journal of Spectroscopy, 2013, Article ID: 927962. [29] Wang, H., Duennwald, M.L., Roberts, B.E., Rozeboom, L.M., Zhang, Y.L., Steele, A.D., et al. (2008) Direct and Selective Elimination of Specific Prions and Amyloids by 4,5-Dianilinophthalimide and Analogs. Proceedings of the National Academy of Sciences, 105, 7159-7164.
http://dx.doi.org/10.1073/pnas.0801934105 [30] Cordeiro, Y., Kraineva, J., Suarez, M.C., Tempesta, A.G., Kelly, J.W., Silva, J.L., Winter, R. and Foguel, D. (2006) Fourier Transform Infrared Spectroscopy Provides a Fingerprint for the Tetramer and for the Aggregates of Transthyretin. Biophysical Journal, 91, 957-967.
http://dx.doi.org/10.1529/biophysj.106.085928 [31] Sulkowaska, A. (2002) Interaction of Drugs with Bovine and Human Serum Albumin. Journal of Molecular Structure, 614, 227-232.
http://dx.doi.org/10.1016/S0022-2860(02)00256-9 [32] Garzon-Rodriguez, W., Vega, A., Sepulveda-Becerra, M., Milton, S., Johnson, D.A., Yatsimirsky, A.K. and Glabe, C.G. (2000) A Conformation Change in the Carboxyl Terminus of Alzheimer’s Aβ(1-40) Accompanies the Transition from Dimer to Fibril as Revealed by Fluorescence Quenching Analysis. Journal of Biological Chemistry, 275, 22645-22649.
http://dx.doi.org/10.1074/jbc.M000756200 [33] Sirotkin, V.A., Zinatullin, A.N., Solomonov, B.N., Faizullin, D.A. and Fedotov, V.D. (2001) Calorimetric and Fourier transform Infrared Spectroscopic Study of Solid Proteins Immersed in Low Water Organic Solvents. Biochimica et Biophysica Acta, 1547, 359-369.
http://dx.doi.org/10.1016/S0167-4838(01)00201-1 [34] Zandomeneghi, G., Krebs, M.R.H., Mccammon, M.G. and Fandrichi, M. (2004) FTIR Reveals Structural Differences between Native b-Sheet Proteins and Amyloid Fibrils. Protein Science, 13, 3314-3321.
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