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Vibrational Studies of Different Human Body Disorders Using FTIR Spectroscopy

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DOI: 10.4236/ojapps.2014.43012    4,941 Downloads   7,027 Views   Citations

ABSTRACT

Some of the important features of the bands occur in the present study. The band called amide A is available in all the diseased and healthy controls and the frequency of the band ranges from 3380 cm﹣1 to 3480.74 cm﹣1. The band due to C-H band and called hydrocarbon band was found only in paralytic and Alzheimer diseased along with normal healthy controls. Carbide band (C=C) is found only in Duchenne muscular dystrophy, paralytic and Alzheimer’s disease patients. Amide I was intact in all disorders with normal persons. Peroxide band (O-O) was found in all the cases of study. Amide IV band was found in paralytic, muscular dystrophy, Alzheimer’s diseases and normal controls. The amide V band was found in Alzheimer’s diseases only. The appearance or disappearance of the bands is a good sign to understand the mechanisms at the molecular level. FTIR spectroscopy may help in the diagnosis of the disease at the early stage of the onset. This spectroscopy can be used nicely for the study of hair, vaginal fluid, nails, urine, mucus, semen, synovial fluid, blood, hemoproteins, skin, and tears for human beings. We can also use it to understand the effect of adulteration on food and paint technology. FTIR is an indicator to explore the changes occurring at molecular level.

Conflicts of Interest

The authors declare no conflicts of interest.

Cite this paper

Kumar, S. ,  , R. , Chaudhary, S. ,  , S. and Jain, D. (2014) Vibrational Studies of Different Human Body Disorders Using FTIR Spectroscopy. Open Journal of Applied Sciences, 4, 103-129. doi: 10.4236/ojapps.2014.43012.

References

[1] Mark, B. (2002) Fourier Transform Infrared Spectroscopy. In: Practicing Oil Analysis-Fourier Transform Infrared Spectroscopy-Machinery Lubrication, Noria Publication, Tula, 1-4.
[2] Whiffen, D.H. (1972) Infrared Spectroscopy. In: Spectroscopy, 2nd Edition, John Wiley & Sons, Inc., New York, 92-107.
[3] Gupta, S.L., Kumar, V. and Sharma, R.C. (2007) Vibrational-Rotational Spectra (Near Infrared Spectroscopy). In: Elements of Spectroscopy, Pragati Prakashan, Meerut, 410-449.
[4] Sturat, B. (1997) Biological Applications of Infrared Spectroscopy. John Wiley & Sons, Chichester, 25-33.
[5] Schmit, J. and Flemming, H.C. (1998) FTIR Spectroscopy in Microbial and Material Analysis. International Biodeterioration & Biodegradation, 41, 1-11.
http://dx.doi.org/10.1016/S0964-8305(98)80002-4
[6] Naumann, D. (1984) Some Ultrastructural Information on Intact, Living Bacterial Cells and Related Cell-Wall Fragments as Given by FTIR. Infrared Physics, 24, 233-238.
[7] Naumann, D., Fijala, V., Labichinski, H. and Giesbrecht, P. (1988) The Rapid Differentiation and Identification of Pathogenic Bacteria Using Fourier Transform Infrared Spectroscopic and Multivariate Statistical Analysis. Journal of Molecular Structure, 174, 165-170.
http://dx.doi.org/10.1016/0022-2860(88)80152-2
[8] Ellis, D.I., Harrigan, G.G. and Goodcare, R. (2003) Its Role in Biomarker Discovery and Gene Function Analysis. In: Goodcare, R. and Harrigan, G.G., Eds., Kluwer Academic, Boston, 111-124.
[9] Krimm, S. and Bandekar, J. (1986) Vibrational Spectroscopy and Conformation of Peptides, Polypeptides and Proteins. Advances in Protein Chemistry, 38, 181-364.
http://dx.doi.org/10.1016/S0065-3233(08)60528-8
[10] Movasaghi, Z., Rehman, S. and Ur Rehman, I. (2008) Fourier Transform Infrared (FTIR) Spectroscopy of Biological Tissues. Applied Spectroscopy Review, 43, 134-179.
[11] Kong, J. and Yu, S. (2007) Fourier Transform Infrared Spectroscopic Analysis of Proteins in Secondary. Acta Biochimica et Biophysica Sinica, 39, 549-559.
[12] Venyaminev, S.Y. and Kalmin, N.H. (1990) Quantitative IR Spectrophotometry of Peptides Compounds in Water (H2O) Solution, I, Spectral Parameters of Amino Acid Residue Absorption Bands. Biopolymers, 30, 1243-1257.
http://dx.doi.org/10.1002/bip.360301309
[13] Chirgadze, Y.N., Fedorov, O.V. and Trushina, N.P. (1975) Estimation of Amino Acid Residue Side-Chain Absorption in Infrared Spectra of Protein Solution in Heavy Water. Biopolymers, 14, 679-694.
http://dx.doi.org/10.1002/bip.1975.360140402
[14] Kanagathara, N., Thirunavukkarasu, M., Jeyanthi, C.E. and Shenabagarajan, P. (2011) FTIR and UV-Visible Spectral Study on Normal Blood Samples. International Journal of Pharmacy and Biological Sciences, 1, 74-80.
[15] Gunasekaran, S., Uthra, D., Sailatha, E. and Anita, B. (2010) FTIR Spectral Study on Jaundice Blood Samples before and after Treatment. Asian Journal of Chemistry, 22, 51-56.
[16] Gunasekaran, S. and Uthra, D. (2008) FTIR and UV-Visible Spectral Study on Normal and Jaundice Blood Samples. Asian Journal of Chemistry, 20, 5695-5703.
[17] Sankari, G., Krishnamoorthy, E., Jayakumaran, S., Gunasekaran, S., Vishnu, P.V., Subramanian, S., Subramaniam, S. and Surapaneni, K.M. (2010) Analysis of Serum Immunoglobulins Using Fourier Transforms Infrared Spectral Measurements. Biology & Medicine, 2, 42-48.
[18] Chou, L.P., Jackson, M., Willian, C.H. and Mantsch, H.H. (1994) Alzheimer’s Disease: Neuritic Plaques and Neurofibrillary Tangles in Human Brain Identified by FTIR Spectroscopy. Proceedings of SPIE 2089, 9th International Conference on Fourier Transform Spectroscopy, Calgary, 104.
http://dx.doi.org./10.1117/12.166733.
[19] Show, R.A., Kotowich, S., Ecysel, H.H., Jackson, M., Thomson, G.T. and Mantsch, H.H. (1995) Arthritis Diagnosis Based upon the Near-Infrared Spectrum of Synovial Fluid. Rheumatology International, 15, 159-165.
http://dx.doi.org/10.1007/BF00301774
[20] Tarbit, I., Perry, E.K., Perry, R.H., Blessed, G. and Tomlinson, B.E. (1980) Hippocampal Freo Amino Acid in Alzheimer’s Disease. Journal of Neurochemistry, 35, 1246-1249.
http://dx.doi.org/10.1111/j.1471-4159.1980.tb07883.x
[21] Mann, D.M.A. and Sinclair, K.G.A. (1971) The Quantitative Assessment of Lipofusion, Cytoplasmic RNA and Molecular Volume in Senile Dementia. Neuropathology and Applied Neurobiology, 4, 129-135.
http://dx.doi.org/10.1111/j.1365-2990.1978.tb00553.x
[22] Benezzeddine, B.L., Cazorla, G. and Melin, A.M. (2009) Validation for Quantification of Immunoglobulins by Fourier Transform Infrared Spectra. Clinical Chemistry and Laboratory Medicine, 47, 83-90.
[23] Smith, K.F., Haris, P.I., Chapman, D., Reid, K.B. and Perkins, S.J. (1994) Beta-Sheet Secondary Structure of the Trimeric Globular Domain of Clq of Complement and Collagen Type VII, and X by Fourier Transform Infrared Spectroscopy and Averaged Structure Predictions. Biochemical Journal, 301, 249-256.
[24] Petibois, C., Cazoria, G., Cassaigne, A. and Déldris, G. (2001) Plasma Protein Contents Determined by Fourier Transform Infrared Spectrometry. Clinical Chemistry, 47, 730-738.
[25] Pistorius, A.M., De Grip, W.J. and Egerova-Zachemyuk, T.A. (2009) Monitoring of Biomass Composition from Microbiological Sources by Means of FTIR Spectroscopy. Biotechnology and Bioengineering, 103, 123-129.
http://dx.doi.org/10.1002/bit.22220
[26] Karadenizli, A., Kolayli, F. and Ergen, K. (2007) A Novel Application of Fourier Transfered Infrared Spectroscopy: Classification of Slime from Staphylococci. Biofouling, 23, 63-71.
[27] Toubas, D., Essendoubi, M., Adt, I., Pinon, J.M., Manfait, M. and Sockalingum, G.D. (2007) FTIR Spectroscopy in Medical Mycology: Applications to the Differentiation and Typing of Candel. Analytical and Bioanalytical Chemistry, 387, 1729-1737.
http://dx.doi.org/10.1007/s00216-006-1005-1
[28] Tiarang, W., Liv, Y., Lan, L., Yan, G., Ming, N.I.E. and Zhou, J. (2009) Conformational Study of Protein in Some Species of Fubarium by FTIR Spectroscopy. Annals of Microbiology, 58, 169-171.
[29] Isa Ksan, H., Turunen, M.J., Rieppo, L., Saarakkala, S., Tanminen, I.S., Rieppo, J., Kröger, H. and Jurvelin, J.S. (2010) Infrared Spectroscopy Indicates Altered Bone Turnover and Remodeling Activity in Renal Osteodystrophy. Journal of Bone and Mineral Research, 25, 1360-1366.
http://dx.doi.org/10.1002/jbmr.10
[30] Becker, K., Lahnam, N.A., Fegeler, W., Proctor, R.A., Peters, G. and Van Eift, C. (2006) Fourier Transform Infrared Spectroscopic Analysis Is a Powerful Tool for Studying the Synamic Changes in Staphylacoccusaureus Small-Colony Variants. Journal of Clinical Microbiology, 44, 3274-3278.
http://dx.doi.org/10.1128/JCM.00847-06
[31] Zwielly, A., Mordechai, S., Sinielnikav, I., Salman, A., Bagomotny, E. and Argev, S. (2010) Advanced Statistical Techniques Applied to Comprehensive FTIR Spectra on Human Colonic Tissues. Medical Physics, 37, 1047-1055.
http://dx.doi.org/10.1118/1.3298013
[32] Dimitrova, M., Ivanova, D., Karamancheva, I., Mileu, A. and Dobreu, I. (2009) Application of FTIR Spectroscopy for Diagnosis of Breast Cancer Tumors. Journal of University of Chemical Technology and Metallurgy, 44, 297-300.
[33] Petibois, C., Cazerla, G., Cassaigne, A. and Déléris, G. (2001) Plasma Protein Contents Determined by Fourier Transform Infrared Spectrometry. Clinical Chemistry, 47, 730-738.
[34] Cooper, F.A. and Knutson, K. (1995) Fourier Transform Infrared Spectroscopy Investigations of Protein Structure. Pharmaceutical Biotechnology, 7, 101-143.
http://dx.doi.org/10.1007/978-1-4899-1079-0_3
[35] Buijsand, J. and Nerde, W. (1996) Changes in the Secondary Structure of Adsorbed IgG and F(ab’)2 Studied by FTIR Spectroscopy. Langmuir, 12, 1605-1613.
http://dx.doi.org/10.1021/la950665s
[36] Marco, V.D., Parvez, I.H., Wim, E.H. and Daan, J.A.C. (2001) Fourier Transform Infrared Spectrometric Analysis of Protein Conformation: Effect of Sampling Method and Stress Factors. Analytical Biochemistry, 297, 160-169.
http://dx.doi.org/10.1006/abio.2001.5337
[37] Mackanos, M.A. and Contag, C.H. (2009) FTIR Micro Spectroscopy for Improved Prostate Cancer Diagnosis. Trends in Biotechnology, 27, 661-663.
http://dx.doi.org/10.1016/j.tibtech.2009.09.001
[38] Ebestein, D.M., Coughlin, D., Chapman, J. and Licand Pruitt, L.A. (2009) Nonmechanical Proterties of Calcification, Figrous Tissue, and Hematoma from Atherosclerotic Plaques. Journal of Biomedical Materials Research Part A, 91, 1028-1037.
http://dx.doi.org/10.1002/jbm.a.32321
[39] Zhang, J., Wang, G.Z., Jiang, N., Yang, J.W., Gu, Y. and Fang, Y. (2010) Analysis of Urinary Calculi Composition by Infrared Spectroscopy: A Prospective Study of 625 Patients in Estern China. Urological Research, 38, 111-115.
http://dx.doi.org/10.1007/s00240-010-0253-x
[40] Sossé, D.P., Aké, M.A., Tiahov, G., Koffi, G., CisséCamara, M., Diohan, F., Yapo, E., Kassayou, S., Peuchant, E., Essiagne, S.D. and Mannet, D. (2010) Gall Stone Biochemical Characteristics Using Fourier Transform Infrared Spectroscopy Method. Annales de Biologie Clinique (Paris), 68, 39-42.
[41] Renuga, D.T.S., Gunasekaran, S., Hudson, J.W. and Joybell, I.S.A. (2009) Analysis of Renal Failure Patients Blood Samples: Characterization and Efficacy Study. Indian Journal of Science and Technology, 2, 46-50.
[42] Haas, S.L., Möller, R., Fernandes, A., Dzeyk-Boycheva, K., Wörl, S., Hohmann, J., Hemberger, S., Elmas, E., Brökhmann, M., Bugert, P. and Backhaus, J. (2010) Spectroscopic Diagnosis of Myocardial Infarction and Heart Failure by Fourier Transforms Infrared Spectroscopy in Serum Samples. Applied Spectroscopy, 64, 262-267.
http://dx.doi.org/10.1366/000370210790918508
[43] Malins, D.C., Polissar, N.L., Niohikila, K., Holmes, E.H., Gardner, H.S. and Gunselman, S.J. (1995) The Etiology and Prediction of Breast Cancer. Fourier Transform Infrared Spectroscopy Reveals Progressive Alterations in Breast DNA Leading to a Cancel-Like Phemotype in a High Proportion of Normal Woman. Cancer, 75, 503-517.
http://dx.doi.org/10.1002/1097-0142(19950115)75:2<503::AID-CNCR2820750213>3.0.CO;2-0
[44] Elliott, A. and Ambrose, E.J. (1950) Structure of Synthetic Polypeptides. Nature, 165, 921-922.
http://dx.doi.org/10.1038/165921a0
[45] Timasheff, S.N. and Susi, H. (1966) Infrared Investigations of the Secondary Structure of β-Lactoglobulins. Journal of Biological Chemistry, 241, 249-251.
[46] Pauling, L. and Corey, R.B. (1951) Configurations of Polyplptide Chains with Favored Orientations around Single Bonds: Two New Pleated Sheets. Proceedings of the National Academy of Sciences of the United States of America, 37, 729-740.
http://dx.doi.org/10.1073/pnas.37.11.729
[47] Susi, H. and Byler, D.M. (1983) Protein Structure by Fourier Transform Spectroscopy: Second Derivative Spectra. Biochemical and Biophysical Research Communications, 115, 391-397.
http://dx.doi.org/10.1016/0006-291X(83)91016-1
[48] Krimm, S. and Yasuaki, A. (1972) Intermolecular Interaction Effects in the Amide I Vibrations of β-Poly Peptides. Proceedings of the National Academy of Sciences of the United States of America, 69, 2788-2792.
http://dx.doi.org/10.1073/pnas.69.10.2788
[49] Miyazawa, T. (1960) Perturbation Treatment of the Characteristic Vibrations of Polypeptide Chains in Various Configurations. Journal of Chemical Physics, 32, 1647-1656.
http://dx.doi.org/10.1063/1.1730999
[50] Byler, D.M. and Susi, H. (1986) Examination of the Secondary Structure of Proteins by Deconvolved FTIR Spectra. Biopolymers, 25, 469-487.
http://dx.doi.org/10.1002/bip.360250307
[51] Mantsch, H.H., Heetor, L.C. and Tones, R.N. (1986) Resolution Enhancement of Infrared Spectra of Biological Systems. In: Clark, R.J.H. and Hester, R.E., Eds., Spectroscopy of Biological System, Advances in Spectroscopy, Vol. 13, John Willey & Sons, New York, 16-45.
[52] Hudson, L. and Hay, F.C. (1980) Practical Immunology. 2nd Edition, Blackwell Scientific Publications, Oxford, 222.
[53] Dong, A., Huang, P. and Caughey, W.S. (1990) Protein Secondary Structures in Water from Second-Derivative Amide I Infrared Spectra. Biochemistry, 29, 3303-3308.
http://dx.doi.org/10.1021/bi00465a022
[54] Abaturov, L.V., Nezlin, R.S., Vengerova, T.I. and Varshavsky Jr., M. (1969) Conformational Studies of Immunoglobulin Gand Its Sub Units by the Method of Hydrogen-Deutrium Exchange and Infrared Spectroscopy. Biochimica et Biophysica Acta, 194, 386-396.
http://dx.doi.org/10.1016/0005-2795(69)90099-3

  
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