Abstract

This study presents an application of infrared spectroscopy of sera for monitoring the efficacy of anti-TNFα therapy for inflammatory bowel diseases. Understanding the therapeutic response includes the analysis of absorption bands representing constituent molecules. Interleukin-10 knockout mouse model of the diseases with anti-TNFα treatment was used. The discrimination potential is optimized by analyzing data with curve fitting. It shows; antibody therapy markedly ameliorated the disease, concurring with earlier mucosal immunology and pathophysiologic studies. This technique may thus also be useful for the evaluation of mucosal healing or other therapeutic modalities of gastrointestinal tract diseases keeping the endoscopic tests as confirmatory.

© 2020 Optical Society of America under the terms of the OSA Open Access Publishing Agreement

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2020 (2)

P. J. Koelink, F. M. Bloemendaal, B. Li, L. Westera, E. W. Vogels, M. van Roest, A. K. Gloudemans, A. V. vant Wout, H. Korf, S. Vermeiere, A. A. te Velde, C. Y. Ponsioen, G. R. D Haens, J. S. Verbeek, T. L. Geiger, M. E. Wildenberg, and G. R. van den Brink, “Anti-TNF therapy in IBD exerts its therapeutic effect through macrophage IL-10 signalling,” Gut 69(6), 1053–1063 (2020).
[Crossref]

H. Ghimire, C. Garlapati, E. A. Janssen, U. Krishnamurti, G. Qin, R. Aneja, and A. G. Unil Perera, “Protein Conformational Changes in Breast Cancer Sera Using Infrared Spectroscopic Analysis,” Cancers 12(7), 1708 (2020).
[Crossref]

2019 (2)

K. Aden, A. Rehman, S. Waschina, W.-H. Pan, A. Walker, M. Lucio, A. M. Munez, R. Bharti, J. Zimmerman, J. Bethge, B. Schulte, B. Schulte, A. Franke, S. Nikolaus, J. O. Shroeder, D. Vandeputte, J. Raes, S. Szymczak, and P. Rosenstiel, “Metabolic functions of gut microbes associate with efficacy of tumor necrosis factor antagonists in patients with inflammatory bowel diseases,” Gastroenterology 157(5), 1279–1292.e11 (2019).
[Crossref]

H. Ghimire, P. Jayaweera, and A. U. Perera, “Longitudinal analysis of molecular alteration in serum samples of dextran sodium sulfate-induced colitis mice by using infrared spectroscopy,” Infrared Phys. Technol. 97, 33–37 (2019).
[Crossref]

2018 (2)

J. Titus, H. Ghimire, E. Viennois, D. Merlin, and A. Unil Perera, “Protein secondary structure analysis of dried blood serum using infrared spectroscopy to identify markers for colitis screening,” J. Biophotonics 11(3), e201700057 (2018).
[Crossref]

E. A. Scoville, M. M. Allaman, C. T. Brown, A. K. Motley, S. N. Horst, C. S. Williams, T. Koyama, Z Zhao, D. Beaulieu, K. T. Wilson, and L. A. Coburn, “Alterations in lipid, amino acid, and energy metabolism distinguish Crohn’s disease from ulcerative colitis and control subjects by serum metabolomic profiling,” Metabolomics 14(1), 17 (2018).
[Crossref]

2017 (4)

H. Ghimire, M. Venkataramani, Z. Bian, Y. Liu, and A. U. Perera, “ATR-FTIR spectral discrimination between normal and tumorous mouse models of lymphoma and melanoma from serum samples,” Sci. Rep. 7(1), 1–9 (2017).
[Crossref]

J. Titus, E. Viennois, D. Merlin, and A. Unil Perera, “Minimally invasive screening for colitis using attenuated total internal reflectance fourier transform infrared spectroscopy,” J. Biophotonics 10(3), 465–472 (2017).
[Crossref]

W. E. Ip, N. Hoshi, D. S. Shouval, S. Snapper, and R. Medzhitov, “Anti-inflammatory effect of IL-10 mediated by metabolic reprogramming of macrophages,” Science 356(6337), 513–519 (2017).
[Crossref]

E. Viennois, Y. Zhao, M. K. Han, B. Xiao, M. Zhang, M. Prasad, L. Wang, and D. Merlin, “Serum miRNA signature diagnoses and discriminates murine colitis subtypes and predicts ulcerative colitis in humans,” Sci. Rep. 7(1), 2520 (2017).
[Crossref]

2016 (2)

K. A. Chan and S. G. Kazarian, “Attenuated total reflection Fourier-transform infrared (ATR-FTIR) imaging of tissues and live cells,” Chem. Soc. Rev. 45(7), 1850–1864 (2016).
[Crossref]

D. M. Wiese, S. N. Horst, C. T. Brown, M. M. Allaman, M. E. Hodges, J. C. Slaughter, J. P. Druce, D. B. Beaulieu, D. A. Schwartz, K. T. Wilson, and L. A. Coburn, “Serum fatty acids are correlated with inflammatory cytokines in ulcerative colitis,” PLoS One 11(5), e0156387 (2016).
[Crossref]

2015 (2)

H. Yang, S. Yang, J. Kong, A. Dong, and S. Yu, “Obtaining information about protein secondary structures in aqueous solution using Fourier transform IR spectroscopy,” Nat. Protoc. 10(3), 382–396 (2015).
[Crossref]

E. Viennois, M. T. Baker, B. Xiao, L. Wang, H. Laroui, and D. Merlin, “Longitudinal study of circulating protein biomarkers in inflammatory bowel disease,” J. Proteomics 112, 166–179 (2015).
[Crossref]

2014 (4)

M. J. Baker, J. Trevisan, P. Bassan, R. Bhargava, H. J. Butler, K. M. Dorling, P. R. Fielden, S. W. Fogarty, N. J. Fullwood, K. A. Heys, C. Hughes, P. Lasch, P. L. Martin-Hirsch, B. Obinaju, G. D. Sockalingum, J. Sulé-Suso, R. J. Strong, M. J. Walsh, B. R. Wood, P. Gardner, and F. L. Martin, “Using Fourier transform IR spectroscopy to analyze biological materials,” Nat. Protoc. 9(8), 1771–1791 (2014).
[Crossref]

J. Pedersen, M. Coskun, C. Soendergaard, M. Salem, and O. H. Nielsen, “Inflammatory pathways of importance for management of inflammatory bowel disease,” World J. Gastroentero. 20(1), 64 (2014).
[Crossref]

G. Clemens, J. R. Hands, K. M. Dorling, and M. J. Baker, “Vibrational spectroscopic methods for cytology and cellular research,” Analyst 139(18), 4411–4444 (2014).
[Crossref]

P. Ramalingam, Y. P. Reddy, K. V. Kumar, B. R. Chandu, and K. Rajendran, “Evaluation of metformin hydrochloride in Wistar rats by FTIR-ATR spectroscopy: A convenient tool in the clinical study of diabetes,” J. Nat. Sc. Biol. Med. 5(2), 288 (2014).
[Crossref]

2013 (3)

P. I. Haris, “Probing protein–protein interaction in biomembranes using Fourier transform infrared spectroscopy,” Biochim. Biophys. Acta, Biomembr. 1828(10), 2265–2271 (2013).
[Crossref]

A. Tesija Kuna, “Serological markers of inflammatory bowel disease,” Biochem. Med. 23(1), 28–42 (2013).
[Crossref]

S. G. Kazarian and K. A. Chan, “ATR-FTIR spectroscopic imaging: recent advances and applications to biological systems,” Analyst 138(7), 1940–1951 (2013).
[Crossref]

2012 (1)

M. Dave and E. V. Loftus Jr, “Mucosal healing in inflammatory bowel disease—a true paradigm of success?” Gastroenterology & hepatology 8(1), 29 (2012).

2010 (3)

L. Peyrin-Biroulet, “Anti-TNF therapy in inflammatory bowel diseases: a huge review,” Minerva gastroenterologica e dietologica 56(2), 233–243 (2010).

S. G. Kazarian and K. A. Chan, “Micro-and macro-attenuated total reflection Fourier transform infrared spectroscopic imaging,” Appl. Spectrosc. 64(5), 135A–152A (2010).
[Crossref]

P. D. Lewis, K. E. Lewis, R. Ghosal, S. Bayliss, A. J. Lloyd, J. Wills, R. Godfrey, P. Kloer, and L. A. Mur, “Evaluation of FTIR spectroscopy as a diagnostic tool for lung cancer using sputum,” BMC Cancer 10(1), 640 (2010).
[Crossref]

2009 (3)

Å. Rinnan, F. van den Berg, and S. B. Engelsen, “Review of the most common pre-processing techniques for near-infrared spectra,” TrAC, Trends Anal. Chem. 28(10), 1201–1222 (2009).
[Crossref]

J. Barahona-Garrido, H. Sarti, M. Barahona-Garrido, J. Hernández-Calleros, E. Coss-Adame, and S. Garcia-Saenz et al., “Serological markers in inflammatory bowel disease: a review of their clinical utility,” Revista de gastroenterologia de Mexico 74(3), 230–237 (2009).

A.-M. Šimundić, “Measures of diagnostic accuracy: basic definitions,” EJIFCC 19(4), 203 (2009).

2008 (4)

Z. Movasaghi, S. Rehman, and D. I. ur Rehman, “Fourier transform infrared (FTIR) spectroscopy of biological tissues,” Appl. Spectrosc. Rev. 43(2), 134–179 (2008).
[Crossref]

M. J. Baker, E. Gazi, M. D. Brown, J. H. Shanks, P. Gardner, and N. W. Clarke, “FTIR-based spectroscopic analysis in the identification of clinically aggressive prostate cancer,” Br. J. Cancer 99(11), 1859–1866 (2008).
[Crossref]

L. Hancock and N. Mortensen, “How often do IBD patients require resection of their intestine?” Inflammatory Bowel Dis. 14(suppl_2), S68–S69 (2008).
[Crossref]

A. R. Green, A. Peters-Lewis, S. Percac-Lima, J. R. Betancourt, J. M. Richter, M.-P. R. Janairo, G. Gamba, and S. A. Atlas, “Barriers to screening colonoscopy for low-income Latino and white patients in an urban community health center,” J. Gen. Intern. Med. 23(6), 834–840 (2008).
[Crossref]

2007 (5)

D. N. Frank, A. L. S. Amand, R. A. Feldman, E. C. Boedeker, N. Harpaz, and N. R. Pace, “Molecular-phylogenetic characterization of microbial community imbalances in human inflammatory bowel diseases,” Proc. Natl. Acad. Sci. 104(34), 13780–13785 (2007).
[Crossref]

D. A. Naylor and M. K. Tahic, “Apodizing functions for Fourier transform spectroscopy,” J. Opt. Soc. Am. A 24(11), 3644–3648 (2007).
[Crossref]

M. Szczerbowska-Boruchowska, P. Dumas, M. Z. Kastyak, J. Chwiej, M. Lankosz, D. Adamek, and A. Krygowska-Wajs, “Biomolecular investigation of human substantia nigra in Parkinson’s disease by synchrotron radiation Fourier transform infrared microspectroscopy,” Arch. Biochem. Biophys. 459(2), 241–248 (2007).
[Crossref]

A. Yamanaka, A. Hashimoto, T. Matsuo, M. Kanou, K.-I. Suehara, and T. Kameoka, “Analysis of kinetic uptake phenomena of monosaccharide and disaccharide by suspension TBY-2 cells using an FT-IR/ATR method,” Bioprocess Biosyst. Eng. 30(6), 457–468 (2007).
[Crossref]

J. Kong and S. Yu, “Fourier transform infrared spectroscopic analysis of protein secondary structures,” Acta Biochim. Biophys. Sin. 39(8), 549–559 (2007).
[Crossref]

2006 (1)

S. Rakoff-Nahoum, L. Hao, and R. Medzhitov, “Role of toll-like receptors in spontaneous commensal-dependent colitis,” Immunity 25(2), 319–329 (2006).
[Crossref]

2005 (1)

J. B. Reitsma, A. S. Glas, A. W. Rutjes, R. J. Scholten, P. M. Bossuyt, and A. H. Zwinderman, “Bivariate analysis of sensitivity and specificity produces informative summary measures in diagnostic reviews,” J. Chronic Dis. 58(10), 982–990 (2005).
[Crossref]

2004 (3)

R. Sahu, S. Argov, A. Salman, M. Huleihel, N. Grossman, Z. Hammody, J. Kapelushnik, and S. Mordechai, “Characteristic absorbance of nucleic acids in the Mid-IR region as possible common biomarkers for diagnosis of malignancy,” Technol. Cancer Res. Treat. 3(6), 629–638 (2004).
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S. H. Itzkowitz and X. Yio, “Inflammation and cancer IV. Colorectal cancer in inflammatory bowel disease: the role of inflammation,” Am. J. Physiol. Gastrointest. Liver Physiol. 287(1), G7–G17 (2004).
[Crossref]

D. W. Hommes and S. J. J. G. van Deventer, “Endoscopy in inflammatory bowel diseases,” Gastroenterology 126(6), 1561–1573 (2004).
[Crossref]

2003 (1)

T. Scheinin, D. M. Butler, F. Salway, B. Scallon, and M. Feldmann, “Validation of the interleukin-10 knockout mouse model of colitis: antitumour necrosis factor-antibodies suppress the progression of colitis,” Clin. Exp. Immunol. 133(1), 38–43 (2003).
[Crossref]

2002 (2)

A. Akazawa, I. Sakaida, S. Higaki, Y. Kubo, K. Uchida, and K. Okita, “Increased expression of tumor necrosis factor-α messenger RNA in the intestinal mucosa of inflammatory bowel disease, particularly in patients with disease in the inactive phase,” J. Gastroenterol. 37(5), 345–353 (2002).
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J. Grdadolnik, “ATR-FTIR spectroscopy: Its advantage and limitations,” Acta Chimica Slovenica 49(3), 631–642 (2002).

2001 (1)

Ø. Hammer, D. A. Harper, and P. D. Ryan, “PAST: Paleontological statistics software package for education and data analysis,” Palaeontologia electronica 4(1), 9 (2001).

2000 (2)

J. T. Pelton and L. R. McLean, “Spectroscopic Methods for Analysis of Protein Secondary Structure,” Anal. Biochem. 277(2), 167–176 (2000).
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G. I. Dovbeshko, N. Y. Gridina, E. B. Kruglova, and O. P. Pashchuk, “FTIR spectroscopy studies of nucleic acid damage,” Talanta 53(1), 233–246 (2000).
[Crossref]

1999 (2)

C. Petibois, V. Rigalleau, A.-M. Melin, A. Perromat, G. Cazorla, H. Gin, and H. Deleris, “Determination of glucose in dried serum samples by Fourier-transform infrared spectroscopy,” Clin. Chem. 45(9), 1530–1535 (1999).
[Crossref]

A. Tagore, W. Gonsalkorale, V. Pravica, A. Hajeer, R. McMahon, P. Whorwell, P. J. Sinnott, and I. V. Hutchinson, “Interleukin-10 (IL-10) genotypes in inflammatory bowel disease,” Tissue Antigens 54(4), 386–390 (1999).
[Crossref]

1998 (2)

B. R. Wood, M. A. Quinn, F. R. Burden, and D. McNaughton, “An investigation into FTIR spectroscopy as a biodiagnostic tool for cervical cancer,” Biospectroscopy 2(3), 143–153 (1998).
[Crossref]

P. G. Andrus and R. D. Strickland, “Cancer grading by Fourier transform infrared spectroscopy,” Biospectroscopy 4(1), 37–46 (1998).
[Crossref]

1996 (1)

L.-P. i. Choo, D. L. Wetzel, W. C. Halliday, M. Jackson, S. M. LeVine, and H. H. Mantsch, “In situ characterization of beta-amyloid in Alzheimer's diseased tissue by synchrotron Fourier transform infrared microspectroscopy,” Biophys. J. 71(4), 1672–1679 (1996).
[Crossref]

1995 (2)

H. M. Van Dullemen, S. J. van Deventer, D. W. Hommes, H. A. Bijl, J. Jansen, G. N. Tytgat, and J. Woody, “Treatment of Crohn's disease with anti-tumor necrosis factor chimeric monoclonal antibody (cA2),” Gastroenterology 109(1), 129–135 (1995).
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H. Fabian, M. Jackson, L. Murphy, P. H. Watson, I. Fichtner, and H. H. Mantsch, “A comparative infrared spectroscopic study of human breast tumors and breast tumor cell xenografts,” Biospectroscopy 1(1), 37–45 (1995).
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1993 (2)

R. Kühn, J. Löhler, D. Rennick, K. Rajewsky, and W. Müller, “Interleukin-10-deficient mice develop chronic enterocolitis,” Cell 75(2), 263–274 (1993).
[Crossref]

R. Pribic, I. Vanstokkum, D. Chapman, P. I. Haris, and M. Bloemendal, “Protein secondary structure from Fourier transform infrared and/or circular dichroism spectra,” Anal. Biochem. 214(2), 366–378 (1993).
[Crossref]

1990 (1)

J. A. Pierce, R. S. Jackson, K. W. Van Every, P. R. Griffiths, and H. Gao, “Combined deconvolution and curve fitting for quantitative analysis of unresolved spectral bands,” Anal. Chem. 62(5), 477–484 (1990).
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1989 (1)

D. K. Rex, J. C. Lappas, D. D. Maglinte, M. C. Malczewski, K. A. Kopecky, and E. M. Cockerill, “Enteroclysis in the evaluation of suspected small intestinal bleeding,” Gastroenterology 97(1), 58–60 (1989).
[Crossref]

1976 (1)

Adamek, D.

M. Szczerbowska-Boruchowska, P. Dumas, M. Z. Kastyak, J. Chwiej, M. Lankosz, D. Adamek, and A. Krygowska-Wajs, “Biomolecular investigation of human substantia nigra in Parkinson’s disease by synchrotron radiation Fourier transform infrared microspectroscopy,” Arch. Biochem. Biophys. 459(2), 241–248 (2007).
[Crossref]

Aden, K.

K. Aden, A. Rehman, S. Waschina, W.-H. Pan, A. Walker, M. Lucio, A. M. Munez, R. Bharti, J. Zimmerman, J. Bethge, B. Schulte, B. Schulte, A. Franke, S. Nikolaus, J. O. Shroeder, D. Vandeputte, J. Raes, S. Szymczak, and P. Rosenstiel, “Metabolic functions of gut microbes associate with efficacy of tumor necrosis factor antagonists in patients with inflammatory bowel diseases,” Gastroenterology 157(5), 1279–1292.e11 (2019).
[Crossref]

Akazawa, A.

A. Akazawa, I. Sakaida, S. Higaki, Y. Kubo, K. Uchida, and K. Okita, “Increased expression of tumor necrosis factor-α messenger RNA in the intestinal mucosa of inflammatory bowel disease, particularly in patients with disease in the inactive phase,” J. Gastroenterol. 37(5), 345–353 (2002).
[Crossref]

Allaman, M. M.

E. A. Scoville, M. M. Allaman, C. T. Brown, A. K. Motley, S. N. Horst, C. S. Williams, T. Koyama, Z Zhao, D. Beaulieu, K. T. Wilson, and L. A. Coburn, “Alterations in lipid, amino acid, and energy metabolism distinguish Crohn’s disease from ulcerative colitis and control subjects by serum metabolomic profiling,” Metabolomics 14(1), 17 (2018).
[Crossref]

D. M. Wiese, S. N. Horst, C. T. Brown, M. M. Allaman, M. E. Hodges, J. C. Slaughter, J. P. Druce, D. B. Beaulieu, D. A. Schwartz, K. T. Wilson, and L. A. Coburn, “Serum fatty acids are correlated with inflammatory cytokines in ulcerative colitis,” PLoS One 11(5), e0156387 (2016).
[Crossref]

Amand, A. L. S.

D. N. Frank, A. L. S. Amand, R. A. Feldman, E. C. Boedeker, N. Harpaz, and N. R. Pace, “Molecular-phylogenetic characterization of microbial community imbalances in human inflammatory bowel diseases,” Proc. Natl. Acad. Sci. 104(34), 13780–13785 (2007).
[Crossref]

Andrus, P. G.

P. G. Andrus and R. D. Strickland, “Cancer grading by Fourier transform infrared spectroscopy,” Biospectroscopy 4(1), 37–46 (1998).
[Crossref]

Aneja, R.

H. Ghimire, C. Garlapati, E. A. Janssen, U. Krishnamurti, G. Qin, R. Aneja, and A. G. Unil Perera, “Protein Conformational Changes in Breast Cancer Sera Using Infrared Spectroscopic Analysis,” Cancers 12(7), 1708 (2020).
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Argov, S.

R. Sahu, S. Argov, A. Salman, M. Huleihel, N. Grossman, Z. Hammody, J. Kapelushnik, and S. Mordechai, “Characteristic absorbance of nucleic acids in the Mid-IR region as possible common biomarkers for diagnosis of malignancy,” Technol. Cancer Res. Treat. 3(6), 629–638 (2004).
[Crossref]

Atlas, S. A.

A. R. Green, A. Peters-Lewis, S. Percac-Lima, J. R. Betancourt, J. M. Richter, M.-P. R. Janairo, G. Gamba, and S. A. Atlas, “Barriers to screening colonoscopy for low-income Latino and white patients in an urban community health center,” J. Gen. Intern. Med. 23(6), 834–840 (2008).
[Crossref]

Baker, M. J.

M. J. Baker, J. Trevisan, P. Bassan, R. Bhargava, H. J. Butler, K. M. Dorling, P. R. Fielden, S. W. Fogarty, N. J. Fullwood, K. A. Heys, C. Hughes, P. Lasch, P. L. Martin-Hirsch, B. Obinaju, G. D. Sockalingum, J. Sulé-Suso, R. J. Strong, M. J. Walsh, B. R. Wood, P. Gardner, and F. L. Martin, “Using Fourier transform IR spectroscopy to analyze biological materials,” Nat. Protoc. 9(8), 1771–1791 (2014).
[Crossref]

G. Clemens, J. R. Hands, K. M. Dorling, and M. J. Baker, “Vibrational spectroscopic methods for cytology and cellular research,” Analyst 139(18), 4411–4444 (2014).
[Crossref]

M. J. Baker, E. Gazi, M. D. Brown, J. H. Shanks, P. Gardner, and N. W. Clarke, “FTIR-based spectroscopic analysis in the identification of clinically aggressive prostate cancer,” Br. J. Cancer 99(11), 1859–1866 (2008).
[Crossref]

Baker, M. T.

E. Viennois, M. T. Baker, B. Xiao, L. Wang, H. Laroui, and D. Merlin, “Longitudinal study of circulating protein biomarkers in inflammatory bowel disease,” J. Proteomics 112, 166–179 (2015).
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Barahona-Garrido, J.

J. Barahona-Garrido, H. Sarti, M. Barahona-Garrido, J. Hernández-Calleros, E. Coss-Adame, and S. Garcia-Saenz et al., “Serological markers in inflammatory bowel disease: a review of their clinical utility,” Revista de gastroenterologia de Mexico 74(3), 230–237 (2009).

Barahona-Garrido, M.

J. Barahona-Garrido, H. Sarti, M. Barahona-Garrido, J. Hernández-Calleros, E. Coss-Adame, and S. Garcia-Saenz et al., “Serological markers in inflammatory bowel disease: a review of their clinical utility,” Revista de gastroenterologia de Mexico 74(3), 230–237 (2009).

Bassan, P.

M. J. Baker, J. Trevisan, P. Bassan, R. Bhargava, H. J. Butler, K. M. Dorling, P. R. Fielden, S. W. Fogarty, N. J. Fullwood, K. A. Heys, C. Hughes, P. Lasch, P. L. Martin-Hirsch, B. Obinaju, G. D. Sockalingum, J. Sulé-Suso, R. J. Strong, M. J. Walsh, B. R. Wood, P. Gardner, and F. L. Martin, “Using Fourier transform IR spectroscopy to analyze biological materials,” Nat. Protoc. 9(8), 1771–1791 (2014).
[Crossref]

Bayliss, S.

P. D. Lewis, K. E. Lewis, R. Ghosal, S. Bayliss, A. J. Lloyd, J. Wills, R. Godfrey, P. Kloer, and L. A. Mur, “Evaluation of FTIR spectroscopy as a diagnostic tool for lung cancer using sputum,” BMC Cancer 10(1), 640 (2010).
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Beaulieu, D.

E. A. Scoville, M. M. Allaman, C. T. Brown, A. K. Motley, S. N. Horst, C. S. Williams, T. Koyama, Z Zhao, D. Beaulieu, K. T. Wilson, and L. A. Coburn, “Alterations in lipid, amino acid, and energy metabolism distinguish Crohn’s disease from ulcerative colitis and control subjects by serum metabolomic profiling,” Metabolomics 14(1), 17 (2018).
[Crossref]

Beaulieu, D. B.

D. M. Wiese, S. N. Horst, C. T. Brown, M. M. Allaman, M. E. Hodges, J. C. Slaughter, J. P. Druce, D. B. Beaulieu, D. A. Schwartz, K. T. Wilson, and L. A. Coburn, “Serum fatty acids are correlated with inflammatory cytokines in ulcerative colitis,” PLoS One 11(5), e0156387 (2016).
[Crossref]

Betancourt, J. R.

A. R. Green, A. Peters-Lewis, S. Percac-Lima, J. R. Betancourt, J. M. Richter, M.-P. R. Janairo, G. Gamba, and S. A. Atlas, “Barriers to screening colonoscopy for low-income Latino and white patients in an urban community health center,” J. Gen. Intern. Med. 23(6), 834–840 (2008).
[Crossref]

Bethge, J.

K. Aden, A. Rehman, S. Waschina, W.-H. Pan, A. Walker, M. Lucio, A. M. Munez, R. Bharti, J. Zimmerman, J. Bethge, B. Schulte, B. Schulte, A. Franke, S. Nikolaus, J. O. Shroeder, D. Vandeputte, J. Raes, S. Szymczak, and P. Rosenstiel, “Metabolic functions of gut microbes associate with efficacy of tumor necrosis factor antagonists in patients with inflammatory bowel diseases,” Gastroenterology 157(5), 1279–1292.e11 (2019).
[Crossref]

Bhargava, R.

M. J. Baker, J. Trevisan, P. Bassan, R. Bhargava, H. J. Butler, K. M. Dorling, P. R. Fielden, S. W. Fogarty, N. J. Fullwood, K. A. Heys, C. Hughes, P. Lasch, P. L. Martin-Hirsch, B. Obinaju, G. D. Sockalingum, J. Sulé-Suso, R. J. Strong, M. J. Walsh, B. R. Wood, P. Gardner, and F. L. Martin, “Using Fourier transform IR spectroscopy to analyze biological materials,” Nat. Protoc. 9(8), 1771–1791 (2014).
[Crossref]

Bharti, R.

K. Aden, A. Rehman, S. Waschina, W.-H. Pan, A. Walker, M. Lucio, A. M. Munez, R. Bharti, J. Zimmerman, J. Bethge, B. Schulte, B. Schulte, A. Franke, S. Nikolaus, J. O. Shroeder, D. Vandeputte, J. Raes, S. Szymczak, and P. Rosenstiel, “Metabolic functions of gut microbes associate with efficacy of tumor necrosis factor antagonists in patients with inflammatory bowel diseases,” Gastroenterology 157(5), 1279–1292.e11 (2019).
[Crossref]

Bian, Z.

H. Ghimire, M. Venkataramani, Z. Bian, Y. Liu, and A. U. Perera, “ATR-FTIR spectral discrimination between normal and tumorous mouse models of lymphoma and melanoma from serum samples,” Sci. Rep. 7(1), 1–9 (2017).
[Crossref]

Bijl, H. A.

H. M. Van Dullemen, S. J. van Deventer, D. W. Hommes, H. A. Bijl, J. Jansen, G. N. Tytgat, and J. Woody, “Treatment of Crohn's disease with anti-tumor necrosis factor chimeric monoclonal antibody (cA2),” Gastroenterology 109(1), 129–135 (1995).
[Crossref]

Bloemendaal, F. M.

P. J. Koelink, F. M. Bloemendaal, B. Li, L. Westera, E. W. Vogels, M. van Roest, A. K. Gloudemans, A. V. vant Wout, H. Korf, S. Vermeiere, A. A. te Velde, C. Y. Ponsioen, G. R. D Haens, J. S. Verbeek, T. L. Geiger, M. E. Wildenberg, and G. R. van den Brink, “Anti-TNF therapy in IBD exerts its therapeutic effect through macrophage IL-10 signalling,” Gut 69(6), 1053–1063 (2020).
[Crossref]

Bloemendal, M.

R. Pribic, I. Vanstokkum, D. Chapman, P. I. Haris, and M. Bloemendal, “Protein secondary structure from Fourier transform infrared and/or circular dichroism spectra,” Anal. Biochem. 214(2), 366–378 (1993).
[Crossref]

Boedeker, E. C.

D. N. Frank, A. L. S. Amand, R. A. Feldman, E. C. Boedeker, N. Harpaz, and N. R. Pace, “Molecular-phylogenetic characterization of microbial community imbalances in human inflammatory bowel diseases,” Proc. Natl. Acad. Sci. 104(34), 13780–13785 (2007).
[Crossref]

Bossuyt, P. M.

J. B. Reitsma, A. S. Glas, A. W. Rutjes, R. J. Scholten, P. M. Bossuyt, and A. H. Zwinderman, “Bivariate analysis of sensitivity and specificity produces informative summary measures in diagnostic reviews,” J. Chronic Dis. 58(10), 982–990 (2005).
[Crossref]

Bouguen, G.

G. Bouguen and L. Peyrin-Biroulet, “Surgery for adult Crohn's disease: what is the actual risk?” ed: BMJ Publishing Group, 1178–1181 (2011).

Brown, C. T.

E. A. Scoville, M. M. Allaman, C. T. Brown, A. K. Motley, S. N. Horst, C. S. Williams, T. Koyama, Z Zhao, D. Beaulieu, K. T. Wilson, and L. A. Coburn, “Alterations in lipid, amino acid, and energy metabolism distinguish Crohn’s disease from ulcerative colitis and control subjects by serum metabolomic profiling,” Metabolomics 14(1), 17 (2018).
[Crossref]

D. M. Wiese, S. N. Horst, C. T. Brown, M. M. Allaman, M. E. Hodges, J. C. Slaughter, J. P. Druce, D. B. Beaulieu, D. A. Schwartz, K. T. Wilson, and L. A. Coburn, “Serum fatty acids are correlated with inflammatory cytokines in ulcerative colitis,” PLoS One 11(5), e0156387 (2016).
[Crossref]

Brown, M. D.

M. J. Baker, E. Gazi, M. D. Brown, J. H. Shanks, P. Gardner, and N. W. Clarke, “FTIR-based spectroscopic analysis in the identification of clinically aggressive prostate cancer,” Br. J. Cancer 99(11), 1859–1866 (2008).
[Crossref]

Burden, F. R.

B. R. Wood, M. A. Quinn, F. R. Burden, and D. McNaughton, “An investigation into FTIR spectroscopy as a biodiagnostic tool for cervical cancer,” Biospectroscopy 2(3), 143–153 (1998).
[Crossref]

Butler, D. M.

T. Scheinin, D. M. Butler, F. Salway, B. Scallon, and M. Feldmann, “Validation of the interleukin-10 knockout mouse model of colitis: antitumour necrosis factor-antibodies suppress the progression of colitis,” Clin. Exp. Immunol. 133(1), 38–43 (2003).
[Crossref]

Butler, H. J.

M. J. Baker, J. Trevisan, P. Bassan, R. Bhargava, H. J. Butler, K. M. Dorling, P. R. Fielden, S. W. Fogarty, N. J. Fullwood, K. A. Heys, C. Hughes, P. Lasch, P. L. Martin-Hirsch, B. Obinaju, G. D. Sockalingum, J. Sulé-Suso, R. J. Strong, M. J. Walsh, B. R. Wood, P. Gardner, and F. L. Martin, “Using Fourier transform IR spectroscopy to analyze biological materials,” Nat. Protoc. 9(8), 1771–1791 (2014).
[Crossref]

Cazorla, G.

C. Petibois, V. Rigalleau, A.-M. Melin, A. Perromat, G. Cazorla, H. Gin, and H. Deleris, “Determination of glucose in dried serum samples by Fourier-transform infrared spectroscopy,” Clin. Chem. 45(9), 1530–1535 (1999).
[Crossref]

Chan, K. A.

K. A. Chan and S. G. Kazarian, “Attenuated total reflection Fourier-transform infrared (ATR-FTIR) imaging of tissues and live cells,” Chem. Soc. Rev. 45(7), 1850–1864 (2016).
[Crossref]

S. G. Kazarian and K. A. Chan, “ATR-FTIR spectroscopic imaging: recent advances and applications to biological systems,” Analyst 138(7), 1940–1951 (2013).
[Crossref]

S. G. Kazarian and K. A. Chan, “Micro-and macro-attenuated total reflection Fourier transform infrared spectroscopic imaging,” Appl. Spectrosc. 64(5), 135A–152A (2010).
[Crossref]

Chandu, B. R.

P. Ramalingam, Y. P. Reddy, K. V. Kumar, B. R. Chandu, and K. Rajendran, “Evaluation of metformin hydrochloride in Wistar rats by FTIR-ATR spectroscopy: A convenient tool in the clinical study of diabetes,” J. Nat. Sc. Biol. Med. 5(2), 288 (2014).
[Crossref]

Chapman, D.

R. Pribic, I. Vanstokkum, D. Chapman, P. I. Haris, and M. Bloemendal, “Protein secondary structure from Fourier transform infrared and/or circular dichroism spectra,” Anal. Biochem. 214(2), 366–378 (1993).
[Crossref]

Choo, L.-P. i.

L.-P. i. Choo, D. L. Wetzel, W. C. Halliday, M. Jackson, S. M. LeVine, and H. H. Mantsch, “In situ characterization of beta-amyloid in Alzheimer's diseased tissue by synchrotron Fourier transform infrared microspectroscopy,” Biophys. J. 71(4), 1672–1679 (1996).
[Crossref]

Chwiej, J.

M. Szczerbowska-Boruchowska, P. Dumas, M. Z. Kastyak, J. Chwiej, M. Lankosz, D. Adamek, and A. Krygowska-Wajs, “Biomolecular investigation of human substantia nigra in Parkinson’s disease by synchrotron radiation Fourier transform infrared microspectroscopy,” Arch. Biochem. Biophys. 459(2), 241–248 (2007).
[Crossref]

Clarke, N. W.

M. J. Baker, E. Gazi, M. D. Brown, J. H. Shanks, P. Gardner, and N. W. Clarke, “FTIR-based spectroscopic analysis in the identification of clinically aggressive prostate cancer,” Br. J. Cancer 99(11), 1859–1866 (2008).
[Crossref]

Clemens, G.

G. Clemens, J. R. Hands, K. M. Dorling, and M. J. Baker, “Vibrational spectroscopic methods for cytology and cellular research,” Analyst 139(18), 4411–4444 (2014).
[Crossref]

Coburn, L. A.

E. A. Scoville, M. M. Allaman, C. T. Brown, A. K. Motley, S. N. Horst, C. S. Williams, T. Koyama, Z Zhao, D. Beaulieu, K. T. Wilson, and L. A. Coburn, “Alterations in lipid, amino acid, and energy metabolism distinguish Crohn’s disease from ulcerative colitis and control subjects by serum metabolomic profiling,” Metabolomics 14(1), 17 (2018).
[Crossref]

D. M. Wiese, S. N. Horst, C. T. Brown, M. M. Allaman, M. E. Hodges, J. C. Slaughter, J. P. Druce, D. B. Beaulieu, D. A. Schwartz, K. T. Wilson, and L. A. Coburn, “Serum fatty acids are correlated with inflammatory cytokines in ulcerative colitis,” PLoS One 11(5), e0156387 (2016).
[Crossref]

Cockerill, E. M.

D. K. Rex, J. C. Lappas, D. D. Maglinte, M. C. Malczewski, K. A. Kopecky, and E. M. Cockerill, “Enteroclysis in the evaluation of suspected small intestinal bleeding,” Gastroenterology 97(1), 58–60 (1989).
[Crossref]

Coskun, M.

J. Pedersen, M. Coskun, C. Soendergaard, M. Salem, and O. H. Nielsen, “Inflammatory pathways of importance for management of inflammatory bowel disease,” World J. Gastroentero. 20(1), 64 (2014).
[Crossref]

Coss-Adame, E.

J. Barahona-Garrido, H. Sarti, M. Barahona-Garrido, J. Hernández-Calleros, E. Coss-Adame, and S. Garcia-Saenz et al., “Serological markers in inflammatory bowel disease: a review of their clinical utility,” Revista de gastroenterologia de Mexico 74(3), 230–237 (2009).

D Haens, G. R.

P. J. Koelink, F. M. Bloemendaal, B. Li, L. Westera, E. W. Vogels, M. van Roest, A. K. Gloudemans, A. V. vant Wout, H. Korf, S. Vermeiere, A. A. te Velde, C. Y. Ponsioen, G. R. D Haens, J. S. Verbeek, T. L. Geiger, M. E. Wildenberg, and G. R. van den Brink, “Anti-TNF therapy in IBD exerts its therapeutic effect through macrophage IL-10 signalling,” Gut 69(6), 1053–1063 (2020).
[Crossref]

Dave, M.

M. Dave and E. V. Loftus Jr, “Mucosal healing in inflammatory bowel disease—a true paradigm of success?” Gastroenterology & hepatology 8(1), 29 (2012).

Deleris, H.

C. Petibois, V. Rigalleau, A.-M. Melin, A. Perromat, G. Cazorla, H. Gin, and H. Deleris, “Determination of glucose in dried serum samples by Fourier-transform infrared spectroscopy,” Clin. Chem. 45(9), 1530–1535 (1999).
[Crossref]

Dong, A.

H. Yang, S. Yang, J. Kong, A. Dong, and S. Yu, “Obtaining information about protein secondary structures in aqueous solution using Fourier transform IR spectroscopy,” Nat. Protoc. 10(3), 382–396 (2015).
[Crossref]

Dorling, K. M.

G. Clemens, J. R. Hands, K. M. Dorling, and M. J. Baker, “Vibrational spectroscopic methods for cytology and cellular research,” Analyst 139(18), 4411–4444 (2014).
[Crossref]

M. J. Baker, J. Trevisan, P. Bassan, R. Bhargava, H. J. Butler, K. M. Dorling, P. R. Fielden, S. W. Fogarty, N. J. Fullwood, K. A. Heys, C. Hughes, P. Lasch, P. L. Martin-Hirsch, B. Obinaju, G. D. Sockalingum, J. Sulé-Suso, R. J. Strong, M. J. Walsh, B. R. Wood, P. Gardner, and F. L. Martin, “Using Fourier transform IR spectroscopy to analyze biological materials,” Nat. Protoc. 9(8), 1771–1791 (2014).
[Crossref]

Dovbeshko, G. I.

G. I. Dovbeshko, N. Y. Gridina, E. B. Kruglova, and O. P. Pashchuk, “FTIR spectroscopy studies of nucleic acid damage,” Talanta 53(1), 233–246 (2000).
[Crossref]

Druce, J. P.

D. M. Wiese, S. N. Horst, C. T. Brown, M. M. Allaman, M. E. Hodges, J. C. Slaughter, J. P. Druce, D. B. Beaulieu, D. A. Schwartz, K. T. Wilson, and L. A. Coburn, “Serum fatty acids are correlated with inflammatory cytokines in ulcerative colitis,” PLoS One 11(5), e0156387 (2016).
[Crossref]

Dumas, P.

M. Szczerbowska-Boruchowska, P. Dumas, M. Z. Kastyak, J. Chwiej, M. Lankosz, D. Adamek, and A. Krygowska-Wajs, “Biomolecular investigation of human substantia nigra in Parkinson’s disease by synchrotron radiation Fourier transform infrared microspectroscopy,” Arch. Biochem. Biophys. 459(2), 241–248 (2007).
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Figures (6)

Fig. 1.
Fig. 1. (A) Light-sample interaction and formation of the evanescent wave, which extends into the sample in ATR sampling mode. The beam is then collected by a detector as it exits the crystal. (B) Absorbance spectra and its second derivative curve. The measurement was taken at a resolution of 4 cm-1. (C) Dendrogram tree diagram performed, by using Ward’s algorithm and Euclidian distance measurements of vector normalized second derivative curves within spectral range 1600-1700cm-1. A wide difference can be seen between spectra belonging to control and colitis mouse, compared to the degree of the dissimilarity between controls and treated.
Fig. 2.
Fig. 2. The process of spectral deconvolution. (A) Second derivative spectra of amide I absorbance curve 1600-1700cm-1. (B) Gaussian function energy bands used to obtain a curve that fits the experimental absorption curve. (C) Second derivative spectra of nucleic acids and carbohydrates complex band 1000-1140 cm-1. (D) Deconvolution of the complex band by estimating number and position using minima of second derivatives curve.
Fig. 3.
Fig. 3. Normalized absorbance and p-value calculation. (A) Averaged ATR-FTIR spectra of serum samples, derived from control (Non-Colitis, n=16), treated with anti-TNFα antibody (Treated, n=9) and colitis untreated (Colitis, n=9) mice. These spectra show proper anti-TNFα therapy ameliorate the colitis disease. Inset shows magnification within 1200-1000 cm-1 and 1660-1625 cm-1, which clearly shows how the absorbance curve of anti-TNFα treatment comes close to the control levels. (B) P-value calculation of colitis and treated conditions with control types. P-value is less than 0.05 at various spectral bands while comparing non-colitis and colitis, but it is always greater than 0.05 while comparing non-colitis and treated. The region highlighted by the pink box () is the region with p ≤ 0.05.
Fig. 4.
Fig. 4. Representation of identifying spectral markers. (A) Ensemble average representative of absorbance of wavenumber position 1033 cm-1. (B) Ensemble average representative of absorbance of wavenumber position 1076 cm-1. (C) The ratio of absorption values at wavenumber 1121 cm-1 to 1020 cm-1. (D) The ratio of absorbance at wavenumber 1629 cm-1 to 1737cm-1. (E) The integral values of Gaussian function energy bands representing the α helical structure of protein secondary structure. (F) The integral values of Gaussian function energy bands representing the β pleated sheet structure of protein secondary structure. (G) The integral ratio of α-helix and β-sheet protein secondary structures. It shows the level of β sheet structure increase and α helix drops due to colitis and their resettlement in anti- TNF α therapy mice. (H) The sum of the integral area of GFEBs used to fit the experimental curve in the complex band 1000-1140 cm-1.
Fig. 5.
Fig. 5. (A) The expression levels of TNFα in the Total RNAs extracted from colons. The level of TNFα is quantified by qPCR and it confirms the effect of anti-TNFα therapy. (B) ROC curve for the data obtained from the ratio of the integral area of energy bands representing α-helix and β-sheet protein secondary structures. AUC is 0.95 while comparing colitis and non-colitis, but its value is 0.46 while comparing non-colitis and the treated. High diagnostic accuracy (with AUC = 0.95) can be seen for colitis, but poor diagnostic accuracy (with AUC = 0.46) for the treated.
Fig. 6.
Fig. 6. Schematic of ATR-FTIR spectroscopy integrated with data analysis facility. Micro (µ)-controller (I) controls all the functions within the FTIR instruments, while µ-controller (II) takes care of the spectral response analysis.

Tables (3)

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Table 1. Discriminatory infrared spectral bands, with assignments and their bond vibrations.

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Table 2. Quantified values of identified spectral markers: I1033, I1076, I1121/I1020, I1629/I1737, integral ratio (α/β), and the sum of the integral area of GFEBs used to fit the experimental complex band 1000-1140 cm-1. Tabulated p-values represent a comparison between control and colitis.

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Table 3. Sensitivity, specificity and AUC value calculations of identifying spectral markers.