Abstract

Specific proteins and their aggregates form toxic amyloid plaques and neurofibrillary tangles in the brains of people suffering from neurodegenerative diseases such as Alzheimer’s and Parkinson’s. It is important to study these conformational changes to identify and differentiate these diseases at an early stage so that timely medication is provided to patients. Mid-infrared spectroscopy can be used to monitor these changes by studying the line-shapes and the relative absorbances of amide bands present in proteins. This work focusses on the spectroscopy of the protein, Bovine Serum Albumin as an exemplar, and its aggregates using germanium on silicon waveguides in the 1900–1000 cm−1 (5.3–10.0 µm) spectral region.

Published by The Optical Society under the terms of the Creative Commons Attribution 4.0 License. Further distribution of this work must maintain attribution to the author(s) and the published article's title, journal citation, and DOI.

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    [Crossref]
  21. K. A. Majorek, P. J. Porebski, A. Dayal, M. D. Zimmerman, K. Jablonska, A. J. Stewart, M. Chruszcz, and W. Minor, “Structural and immunologic characterization of bovine, horse, and rabbit serum albumins,” Mol. Immunol. 52(3-4), 174–182 (2012).
    [Crossref]
  22. J. Trevisan, P. P. Angelov, A. D. Scott, P. L. Carmichael, and F. L. Martin, “IRootLab: a free and open-source MATLAB toolbox for vibrational biospectroscopy data analysis,” Bioinformatics 29(8), 1095–1097 (2013).
    [Crossref]
  23. N. Cremades, S. I. Cohen, E. Deas, A. Y. Abramov, A. Y. Chen, A. Orte, M. Sandal, R. W. Clarke, P. Dunne, F. A. Aprile, and C. W. Bertoncini, “Direct observation of the interconversion of normal and toxic forms of α-synuclein,” Cell 149(5), 1048–1059 (2012).
    [Crossref]
  24. V. Della Porta, E. Bramanti, B. Campanella, M. R. Tiné, and C. Duce, “Conformational analysis of bovine serum albumin adsorbed on halloysite nanotubes and kaolinite: A Fourier transform infrared spectroscopy study,” RSC Adv. 6(76), 72386–72398 (2016).
    [Crossref]
  25. G. Devitt, K. Howard, A. Mudher, and S. Mahajan, “Raman spectroscopy: an emerging tool in neurodegenerative disease research and diagnosis,” ACS Chem. Neurosci. 9(3), 404–420 (2018).
    [Crossref]

2019 (4)

V. Mittal, M. Nedeljkovic, L. G. Carpenter, A. Z. Khokhar, H. M. H. Chong, G. Z. Mashanovich, P. N. Bartlett, and J. S. Wilkinson, “Waveguide absorption spectroscopy of bovine serum albumin in the mid-infrared fingerprint region,” ACS Sens. 4(7), 1749–1753 (2019).
[Crossref]

G. Devitt, W. Rice, A. Crisford, I. Nandhakumar, A. Mudher, and S. Mahajan, “Conformational Evolution of Molecular Signatures during Amyloidogenic Protein Aggregation,” ACS Chem. Neurosci. 10(11), 4593–4611 (2019).
[Crossref]

D. Finlayson, C. Rinaldi, and M. J. Baker, “Is infrared spectroscopy ready for the clinic?” Anal. Chem. 91(19), 12117–12128 (2019).
[Crossref]

C. O. Odoli, P. Oduor-Odote, and S. Arason, “The influence of lipid content and pretreatment methods on protein conformation in fish (capelin, Mallotus villosus) during smoking and drying,” Food Sci. Nutr. 7(4), 1446–1454 (2019).
[Crossref]

2018 (7)

A. Nakamura, N. Kaneko, V. L. Villemagne, T. Kato, J. Doecke, V. Doré, C. Fowler, Q. X. Li, R. Martins, C. Rowe, and T. Tomita, “High performance plasma amyloid-β biomarkers for Alzheimer’s disease,” Nature 554(7691), 249–254 (2018).
[Crossref]

A. Nabers, L. Perna, J. Lange, U. Mons, J. Schartner, J. Güldenhaupt, K. U. Saum, S. Janelidze, B. Holleczek, D. Rujescu, and O. Hansson, “Amyloid blood biomarker detects Alzheimer's disease,” EMBO Mol. Med. 10(5), 8763 (2018).
[Crossref]

V. Mittal, M. Nedeljkovic, D. Rowe, G. S. Murugan, and J. S. Wilkinson, “Chalcogenide glass waveguides with paper-based fluidics for mid-infrared absorption spectroscopy,” Opt. Lett. 43(12), 2913–2916 (2018).
[Crossref]

M. Tran, D. Huang, T. Komljenovic, J. Peters, A. Malik, and J. Bowers, “Ultra-low-loss silicon waveguides for heterogeneously integrated silicon/III-V photonics,” Appl. Sci. 8(7), 1139 (2018).
[Crossref]

W. Li, P. Anantha, K. H. Lee, H. D. Qiu, X. Guo, S. C. K. Goh, L. Zhang, H. Wang, R. A. Soref, and C. S. Tan, “Spiral waveguides on germanium-on-silicon nitride platform for mid-IR sensing applications,” IEEE Photonics J. 10(3), 1–7 (2018).
[Crossref]

K. Gallacher, R. W. Millar, U. Griškevičiūte, L. Baldassarre, M. Sorel, M. Ortolani, and D. J. Paul, “Low loss Ge-on-Si waveguides operating in the 8–14 µm atmospheric transmission window,” Opt. Express 26(20), 25667–25675 (2018).
[Crossref]

G. Devitt, K. Howard, A. Mudher, and S. Mahajan, “Raman spectroscopy: an emerging tool in neurodegenerative disease research and diagnosis,” ACS Chem. Neurosci. 9(3), 404–420 (2018).
[Crossref]

2017 (1)

2016 (3)

Á. I. López-Lorente, P. Wang, M. Sieger, E. Vargas Catalan, M. Karlsson, F. Nikolajeff, L. Österlund, and B. Mizaikoff, “Mid-infrared thin-film diamond waveguides combined with tunable quantum cascade lasers for analyzing the secondary structure of proteins,” Phys. Status Solidi A 213(8), 2117–2123 (2016).
[Crossref]

M. Seiger and B. Mizaikoff, “Toward on-chip mid-infrared sensor,” Anal. Chem. 88(11), 5562–5573 (2016).
[Crossref]

V. Della Porta, E. Bramanti, B. Campanella, M. R. Tiné, and C. Duce, “Conformational analysis of bovine serum albumin adsorbed on halloysite nanotubes and kaolinite: A Fourier transform infrared spectroscopy study,” RSC Adv. 6(76), 72386–72398 (2016).
[Crossref]

2015 (4)

R. Lu, W. W. Li, A. Katzir, Y. Raichlin, H. Q. Yu, and B. Mizaikoff, “Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors,” Analyst 140(3), 765–770 (2015).
[Crossref]

V. Mittal, A. Aghajani, L. G. Carpenter, J. C. Gates, J. Butement, P. G. Smith, J. S. Wilkinson, and G. S. Murugan, “Fabrication and characterization of high-contrast mid-infrared GeTe4 channel waveguides,” Opt. Lett. 40(9), 2016–2019 (2015).
[Crossref]

B. S. Moorthy, L. K. Iyer, and E. M. Topp, “Characterizing protein structure, dynamics and conformation in lyophilized solids,” Curr. Pharm. Des. 21(40), 5845–5853 (2015).
[Crossref]

M. Verma, A. Vats, and V. Taneja, “Toxic species in amyloid disorders: Oligomers or mature fibrils,” Ann. Indian Acad. Neurol. 18(2), 138 (2015).
[Crossref]

2013 (1)

J. Trevisan, P. P. Angelov, A. D. Scott, P. L. Carmichael, and F. L. Martin, “IRootLab: a free and open-source MATLAB toolbox for vibrational biospectroscopy data analysis,” Bioinformatics 29(8), 1095–1097 (2013).
[Crossref]

2012 (3)

N. Cremades, S. I. Cohen, E. Deas, A. Y. Abramov, A. Y. Chen, A. Orte, M. Sandal, R. W. Clarke, P. Dunne, F. A. Aprile, and C. W. Bertoncini, “Direct observation of the interconversion of normal and toxic forms of α-synuclein,” Cell 149(5), 1048–1059 (2012).
[Crossref]

Y. C. Chang, V. Paeder, L. Hvozdara, J. M. Hartmann, and H. P. Herzig, “Low-loss germanium strip waveguides on silicon for the mid-infrared,” Opt. Lett. 37(14), 2883–2885 (2012).
[Crossref]

K. A. Majorek, P. J. Porebski, A. Dayal, M. D. Zimmerman, K. Jablonska, A. J. Stewart, M. Chruszcz, and W. Minor, “Structural and immunologic characterization of bovine, horse, and rabbit serum albumins,” Mol. Immunol. 52(3-4), 174–182 (2012).
[Crossref]

2000 (1)

C. Jung, “Insight into protein structure and protein–ligand recognition by Fourier transform infrared spectroscopy,” J. Mol. Recognit. 13(6), 325–351 (2000).
[Crossref]

1986 (1)

S. Krimm and J. Bandekar, “Vibrational spectroscopy and conformation of peptides, polypeptides and proteins,” Adv. Protein Chem. 38, 181–364, Academic Press (1986).
[Crossref]

Abramov, A. Y.

N. Cremades, S. I. Cohen, E. Deas, A. Y. Abramov, A. Y. Chen, A. Orte, M. Sandal, R. W. Clarke, P. Dunne, F. A. Aprile, and C. W. Bertoncini, “Direct observation of the interconversion of normal and toxic forms of α-synuclein,” Cell 149(5), 1048–1059 (2012).
[Crossref]

Aghajani, A.

Anantha, P.

W. Li, P. Anantha, K. H. Lee, H. D. Qiu, X. Guo, S. C. K. Goh, L. Zhang, H. Wang, R. A. Soref, and C. S. Tan, “Spiral waveguides on germanium-on-silicon nitride platform for mid-IR sensing applications,” IEEE Photonics J. 10(3), 1–7 (2018).
[Crossref]

Angelov, P. P.

J. Trevisan, P. P. Angelov, A. D. Scott, P. L. Carmichael, and F. L. Martin, “IRootLab: a free and open-source MATLAB toolbox for vibrational biospectroscopy data analysis,” Bioinformatics 29(8), 1095–1097 (2013).
[Crossref]

Aprile, F. A.

N. Cremades, S. I. Cohen, E. Deas, A. Y. Abramov, A. Y. Chen, A. Orte, M. Sandal, R. W. Clarke, P. Dunne, F. A. Aprile, and C. W. Bertoncini, “Direct observation of the interconversion of normal and toxic forms of α-synuclein,” Cell 149(5), 1048–1059 (2012).
[Crossref]

Arason, S.

C. O. Odoli, P. Oduor-Odote, and S. Arason, “The influence of lipid content and pretreatment methods on protein conformation in fish (capelin, Mallotus villosus) during smoking and drying,” Food Sci. Nutr. 7(4), 1446–1454 (2019).
[Crossref]

Baker, M. J.

D. Finlayson, C. Rinaldi, and M. J. Baker, “Is infrared spectroscopy ready for the clinic?” Anal. Chem. 91(19), 12117–12128 (2019).
[Crossref]

Baldassarre, L.

Bandekar, J.

S. Krimm and J. Bandekar, “Vibrational spectroscopy and conformation of peptides, polypeptides and proteins,” Adv. Protein Chem. 38, 181–364, Academic Press (1986).
[Crossref]

Bartlett, P. N.

V. Mittal, M. Nedeljkovic, L. G. Carpenter, A. Z. Khokhar, H. M. H. Chong, G. Z. Mashanovich, P. N. Bartlett, and J. S. Wilkinson, “Waveguide absorption spectroscopy of bovine serum albumin in the mid-infrared fingerprint region,” ACS Sens. 4(7), 1749–1753 (2019).
[Crossref]

Bertoncini, C. W.

N. Cremades, S. I. Cohen, E. Deas, A. Y. Abramov, A. Y. Chen, A. Orte, M. Sandal, R. W. Clarke, P. Dunne, F. A. Aprile, and C. W. Bertoncini, “Direct observation of the interconversion of normal and toxic forms of α-synuclein,” Cell 149(5), 1048–1059 (2012).
[Crossref]

Bowers, J.

M. Tran, D. Huang, T. Komljenovic, J. Peters, A. Malik, and J. Bowers, “Ultra-low-loss silicon waveguides for heterogeneously integrated silicon/III-V photonics,” Appl. Sci. 8(7), 1139 (2018).
[Crossref]

Bramanti, E.

V. Della Porta, E. Bramanti, B. Campanella, M. R. Tiné, and C. Duce, “Conformational analysis of bovine serum albumin adsorbed on halloysite nanotubes and kaolinite: A Fourier transform infrared spectroscopy study,” RSC Adv. 6(76), 72386–72398 (2016).
[Crossref]

Butement, J.

Campanella, B.

V. Della Porta, E. Bramanti, B. Campanella, M. R. Tiné, and C. Duce, “Conformational analysis of bovine serum albumin adsorbed on halloysite nanotubes and kaolinite: A Fourier transform infrared spectroscopy study,” RSC Adv. 6(76), 72386–72398 (2016).
[Crossref]

Carmichael, P. L.

J. Trevisan, P. P. Angelov, A. D. Scott, P. L. Carmichael, and F. L. Martin, “IRootLab: a free and open-source MATLAB toolbox for vibrational biospectroscopy data analysis,” Bioinformatics 29(8), 1095–1097 (2013).
[Crossref]

Carpenter, L. G.

Chang, Y. C.

Chen, A. Y.

N. Cremades, S. I. Cohen, E. Deas, A. Y. Abramov, A. Y. Chen, A. Orte, M. Sandal, R. W. Clarke, P. Dunne, F. A. Aprile, and C. W. Bertoncini, “Direct observation of the interconversion of normal and toxic forms of α-synuclein,” Cell 149(5), 1048–1059 (2012).
[Crossref]

Chong, H. M. H.

V. Mittal, M. Nedeljkovic, L. G. Carpenter, A. Z. Khokhar, H. M. H. Chong, G. Z. Mashanovich, P. N. Bartlett, and J. S. Wilkinson, “Waveguide absorption spectroscopy of bovine serum albumin in the mid-infrared fingerprint region,” ACS Sens. 4(7), 1749–1753 (2019).
[Crossref]

Chruszcz, M.

K. A. Majorek, P. J. Porebski, A. Dayal, M. D. Zimmerman, K. Jablonska, A. J. Stewart, M. Chruszcz, and W. Minor, “Structural and immunologic characterization of bovine, horse, and rabbit serum albumins,” Mol. Immunol. 52(3-4), 174–182 (2012).
[Crossref]

Clarke, R. W.

N. Cremades, S. I. Cohen, E. Deas, A. Y. Abramov, A. Y. Chen, A. Orte, M. Sandal, R. W. Clarke, P. Dunne, F. A. Aprile, and C. W. Bertoncini, “Direct observation of the interconversion of normal and toxic forms of α-synuclein,” Cell 149(5), 1048–1059 (2012).
[Crossref]

Cohen, S. I.

N. Cremades, S. I. Cohen, E. Deas, A. Y. Abramov, A. Y. Chen, A. Orte, M. Sandal, R. W. Clarke, P. Dunne, F. A. Aprile, and C. W. Bertoncini, “Direct observation of the interconversion of normal and toxic forms of α-synuclein,” Cell 149(5), 1048–1059 (2012).
[Crossref]

Cremades, N.

N. Cremades, S. I. Cohen, E. Deas, A. Y. Abramov, A. Y. Chen, A. Orte, M. Sandal, R. W. Clarke, P. Dunne, F. A. Aprile, and C. W. Bertoncini, “Direct observation of the interconversion of normal and toxic forms of α-synuclein,” Cell 149(5), 1048–1059 (2012).
[Crossref]

Crisford, A.

G. Devitt, W. Rice, A. Crisford, I. Nandhakumar, A. Mudher, and S. Mahajan, “Conformational Evolution of Molecular Signatures during Amyloidogenic Protein Aggregation,” ACS Chem. Neurosci. 10(11), 4593–4611 (2019).
[Crossref]

Dayal, A.

K. A. Majorek, P. J. Porebski, A. Dayal, M. D. Zimmerman, K. Jablonska, A. J. Stewart, M. Chruszcz, and W. Minor, “Structural and immunologic characterization of bovine, horse, and rabbit serum albumins,” Mol. Immunol. 52(3-4), 174–182 (2012).
[Crossref]

Deas, E.

N. Cremades, S. I. Cohen, E. Deas, A. Y. Abramov, A. Y. Chen, A. Orte, M. Sandal, R. W. Clarke, P. Dunne, F. A. Aprile, and C. W. Bertoncini, “Direct observation of the interconversion of normal and toxic forms of α-synuclein,” Cell 149(5), 1048–1059 (2012).
[Crossref]

Della Porta, V.

V. Della Porta, E. Bramanti, B. Campanella, M. R. Tiné, and C. Duce, “Conformational analysis of bovine serum albumin adsorbed on halloysite nanotubes and kaolinite: A Fourier transform infrared spectroscopy study,” RSC Adv. 6(76), 72386–72398 (2016).
[Crossref]

Devitt, G.

G. Devitt, W. Rice, A. Crisford, I. Nandhakumar, A. Mudher, and S. Mahajan, “Conformational Evolution of Molecular Signatures during Amyloidogenic Protein Aggregation,” ACS Chem. Neurosci. 10(11), 4593–4611 (2019).
[Crossref]

G. Devitt, K. Howard, A. Mudher, and S. Mahajan, “Raman spectroscopy: an emerging tool in neurodegenerative disease research and diagnosis,” ACS Chem. Neurosci. 9(3), 404–420 (2018).
[Crossref]

Doecke, J.

A. Nakamura, N. Kaneko, V. L. Villemagne, T. Kato, J. Doecke, V. Doré, C. Fowler, Q. X. Li, R. Martins, C. Rowe, and T. Tomita, “High performance plasma amyloid-β biomarkers for Alzheimer’s disease,” Nature 554(7691), 249–254 (2018).
[Crossref]

Doré, V.

A. Nakamura, N. Kaneko, V. L. Villemagne, T. Kato, J. Doecke, V. Doré, C. Fowler, Q. X. Li, R. Martins, C. Rowe, and T. Tomita, “High performance plasma amyloid-β biomarkers for Alzheimer’s disease,” Nature 554(7691), 249–254 (2018).
[Crossref]

Duce, C.

V. Della Porta, E. Bramanti, B. Campanella, M. R. Tiné, and C. Duce, “Conformational analysis of bovine serum albumin adsorbed on halloysite nanotubes and kaolinite: A Fourier transform infrared spectroscopy study,” RSC Adv. 6(76), 72386–72398 (2016).
[Crossref]

Dunne, P.

N. Cremades, S. I. Cohen, E. Deas, A. Y. Abramov, A. Y. Chen, A. Orte, M. Sandal, R. W. Clarke, P. Dunne, F. A. Aprile, and C. W. Bertoncini, “Direct observation of the interconversion of normal and toxic forms of α-synuclein,” Cell 149(5), 1048–1059 (2012).
[Crossref]

Finlayson, D.

D. Finlayson, C. Rinaldi, and M. J. Baker, “Is infrared spectroscopy ready for the clinic?” Anal. Chem. 91(19), 12117–12128 (2019).
[Crossref]

Fowler, C.

A. Nakamura, N. Kaneko, V. L. Villemagne, T. Kato, J. Doecke, V. Doré, C. Fowler, Q. X. Li, R. Martins, C. Rowe, and T. Tomita, “High performance plasma amyloid-β biomarkers for Alzheimer’s disease,” Nature 554(7691), 249–254 (2018).
[Crossref]

Gallacher, K.

Gates, J. C.

Gawith, C. B.

Goh, S. C. K.

W. Li, P. Anantha, K. H. Lee, H. D. Qiu, X. Guo, S. C. K. Goh, L. Zhang, H. Wang, R. A. Soref, and C. S. Tan, “Spiral waveguides on germanium-on-silicon nitride platform for mid-IR sensing applications,” IEEE Photonics J. 10(3), 1–7 (2018).
[Crossref]

Griškeviciute, U.

Güldenhaupt, J.

A. Nabers, L. Perna, J. Lange, U. Mons, J. Schartner, J. Güldenhaupt, K. U. Saum, S. Janelidze, B. Holleczek, D. Rujescu, and O. Hansson, “Amyloid blood biomarker detects Alzheimer's disease,” EMBO Mol. Med. 10(5), 8763 (2018).
[Crossref]

Guo, X.

W. Li, P. Anantha, K. H. Lee, H. D. Qiu, X. Guo, S. C. K. Goh, L. Zhang, H. Wang, R. A. Soref, and C. S. Tan, “Spiral waveguides on germanium-on-silicon nitride platform for mid-IR sensing applications,” IEEE Photonics J. 10(3), 1–7 (2018).
[Crossref]

Hansson, O.

A. Nabers, L. Perna, J. Lange, U. Mons, J. Schartner, J. Güldenhaupt, K. U. Saum, S. Janelidze, B. Holleczek, D. Rujescu, and O. Hansson, “Amyloid blood biomarker detects Alzheimer's disease,” EMBO Mol. Med. 10(5), 8763 (2018).
[Crossref]

Hartmann, J. M.

Herzig, H. P.

Holleczek, B.

A. Nabers, L. Perna, J. Lange, U. Mons, J. Schartner, J. Güldenhaupt, K. U. Saum, S. Janelidze, B. Holleczek, D. Rujescu, and O. Hansson, “Amyloid blood biomarker detects Alzheimer's disease,” EMBO Mol. Med. 10(5), 8763 (2018).
[Crossref]

Howard, K.

G. Devitt, K. Howard, A. Mudher, and S. Mahajan, “Raman spectroscopy: an emerging tool in neurodegenerative disease research and diagnosis,” ACS Chem. Neurosci. 9(3), 404–420 (2018).
[Crossref]

Huang, D.

M. Tran, D. Huang, T. Komljenovic, J. Peters, A. Malik, and J. Bowers, “Ultra-low-loss silicon waveguides for heterogeneously integrated silicon/III-V photonics,” Appl. Sci. 8(7), 1139 (2018).
[Crossref]

Hvozdara, L.

Iyer, L. K.

B. S. Moorthy, L. K. Iyer, and E. M. Topp, “Characterizing protein structure, dynamics and conformation in lyophilized solids,” Curr. Pharm. Des. 21(40), 5845–5853 (2015).
[Crossref]

Jablonska, K.

K. A. Majorek, P. J. Porebski, A. Dayal, M. D. Zimmerman, K. Jablonska, A. J. Stewart, M. Chruszcz, and W. Minor, “Structural and immunologic characterization of bovine, horse, and rabbit serum albumins,” Mol. Immunol. 52(3-4), 174–182 (2012).
[Crossref]

Janelidze, S.

A. Nabers, L. Perna, J. Lange, U. Mons, J. Schartner, J. Güldenhaupt, K. U. Saum, S. Janelidze, B. Holleczek, D. Rujescu, and O. Hansson, “Amyloid blood biomarker detects Alzheimer's disease,” EMBO Mol. Med. 10(5), 8763 (2018).
[Crossref]

Jung, C.

C. Jung, “Insight into protein structure and protein–ligand recognition by Fourier transform infrared spectroscopy,” J. Mol. Recognit. 13(6), 325–351 (2000).
[Crossref]

Kaneko, N.

A. Nakamura, N. Kaneko, V. L. Villemagne, T. Kato, J. Doecke, V. Doré, C. Fowler, Q. X. Li, R. Martins, C. Rowe, and T. Tomita, “High performance plasma amyloid-β biomarkers for Alzheimer’s disease,” Nature 554(7691), 249–254 (2018).
[Crossref]

Karlsson, M.

Á. I. López-Lorente, P. Wang, M. Sieger, E. Vargas Catalan, M. Karlsson, F. Nikolajeff, L. Österlund, and B. Mizaikoff, “Mid-infrared thin-film diamond waveguides combined with tunable quantum cascade lasers for analyzing the secondary structure of proteins,” Phys. Status Solidi A 213(8), 2117–2123 (2016).
[Crossref]

Kato, T.

A. Nakamura, N. Kaneko, V. L. Villemagne, T. Kato, J. Doecke, V. Doré, C. Fowler, Q. X. Li, R. Martins, C. Rowe, and T. Tomita, “High performance plasma amyloid-β biomarkers for Alzheimer’s disease,” Nature 554(7691), 249–254 (2018).
[Crossref]

Katzir, A.

R. Lu, W. W. Li, A. Katzir, Y. Raichlin, H. Q. Yu, and B. Mizaikoff, “Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors,” Analyst 140(3), 765–770 (2015).
[Crossref]

Khokhar, A. Z.

V. Mittal, M. Nedeljkovic, L. G. Carpenter, A. Z. Khokhar, H. M. H. Chong, G. Z. Mashanovich, P. N. Bartlett, and J. S. Wilkinson, “Waveguide absorption spectroscopy of bovine serum albumin in the mid-infrared fingerprint region,” ACS Sens. 4(7), 1749–1753 (2019).
[Crossref]

M. Nedeljkovic, J. S. Penades, V. Mittal, G. S. Murugan, A. Z. Khokhar, C. Littlejohns, L. G. Carpenter, C. B. Gawith, J. S. Wilkinson, and G. Z. Mashanovich, “Germanium-on-silicon waveguides operating at mid-infrared wavelengths up to 8.5 µm,” Opt. Express 25(22), 27431–27441 (2017).
[Crossref]

Komljenovic, T.

M. Tran, D. Huang, T. Komljenovic, J. Peters, A. Malik, and J. Bowers, “Ultra-low-loss silicon waveguides for heterogeneously integrated silicon/III-V photonics,” Appl. Sci. 8(7), 1139 (2018).
[Crossref]

Krimm, S.

S. Krimm and J. Bandekar, “Vibrational spectroscopy and conformation of peptides, polypeptides and proteins,” Adv. Protein Chem. 38, 181–364, Academic Press (1986).
[Crossref]

Lange, J.

A. Nabers, L. Perna, J. Lange, U. Mons, J. Schartner, J. Güldenhaupt, K. U. Saum, S. Janelidze, B. Holleczek, D. Rujescu, and O. Hansson, “Amyloid blood biomarker detects Alzheimer's disease,” EMBO Mol. Med. 10(5), 8763 (2018).
[Crossref]

Lee, K. H.

W. Li, P. Anantha, K. H. Lee, H. D. Qiu, X. Guo, S. C. K. Goh, L. Zhang, H. Wang, R. A. Soref, and C. S. Tan, “Spiral waveguides on germanium-on-silicon nitride platform for mid-IR sensing applications,” IEEE Photonics J. 10(3), 1–7 (2018).
[Crossref]

Li, Q. X.

A. Nakamura, N. Kaneko, V. L. Villemagne, T. Kato, J. Doecke, V. Doré, C. Fowler, Q. X. Li, R. Martins, C. Rowe, and T. Tomita, “High performance plasma amyloid-β biomarkers for Alzheimer’s disease,” Nature 554(7691), 249–254 (2018).
[Crossref]

Li, W.

W. Li, P. Anantha, K. H. Lee, H. D. Qiu, X. Guo, S. C. K. Goh, L. Zhang, H. Wang, R. A. Soref, and C. S. Tan, “Spiral waveguides on germanium-on-silicon nitride platform for mid-IR sensing applications,” IEEE Photonics J. 10(3), 1–7 (2018).
[Crossref]

Li, W. W.

R. Lu, W. W. Li, A. Katzir, Y. Raichlin, H. Q. Yu, and B. Mizaikoff, “Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors,” Analyst 140(3), 765–770 (2015).
[Crossref]

Littlejohns, C.

López-Lorente, Á. I.

Á. I. López-Lorente, P. Wang, M. Sieger, E. Vargas Catalan, M. Karlsson, F. Nikolajeff, L. Österlund, and B. Mizaikoff, “Mid-infrared thin-film diamond waveguides combined with tunable quantum cascade lasers for analyzing the secondary structure of proteins,” Phys. Status Solidi A 213(8), 2117–2123 (2016).
[Crossref]

Lu, R.

R. Lu, W. W. Li, A. Katzir, Y. Raichlin, H. Q. Yu, and B. Mizaikoff, “Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors,” Analyst 140(3), 765–770 (2015).
[Crossref]

Mahajan, S.

G. Devitt, W. Rice, A. Crisford, I. Nandhakumar, A. Mudher, and S. Mahajan, “Conformational Evolution of Molecular Signatures during Amyloidogenic Protein Aggregation,” ACS Chem. Neurosci. 10(11), 4593–4611 (2019).
[Crossref]

G. Devitt, K. Howard, A. Mudher, and S. Mahajan, “Raman spectroscopy: an emerging tool in neurodegenerative disease research and diagnosis,” ACS Chem. Neurosci. 9(3), 404–420 (2018).
[Crossref]

Majorek, K. A.

K. A. Majorek, P. J. Porebski, A. Dayal, M. D. Zimmerman, K. Jablonska, A. J. Stewart, M. Chruszcz, and W. Minor, “Structural and immunologic characterization of bovine, horse, and rabbit serum albumins,” Mol. Immunol. 52(3-4), 174–182 (2012).
[Crossref]

Malik, A.

M. Tran, D. Huang, T. Komljenovic, J. Peters, A. Malik, and J. Bowers, “Ultra-low-loss silicon waveguides for heterogeneously integrated silicon/III-V photonics,” Appl. Sci. 8(7), 1139 (2018).
[Crossref]

Martin, F. L.

J. Trevisan, P. P. Angelov, A. D. Scott, P. L. Carmichael, and F. L. Martin, “IRootLab: a free and open-source MATLAB toolbox for vibrational biospectroscopy data analysis,” Bioinformatics 29(8), 1095–1097 (2013).
[Crossref]

Martins, R.

A. Nakamura, N. Kaneko, V. L. Villemagne, T. Kato, J. Doecke, V. Doré, C. Fowler, Q. X. Li, R. Martins, C. Rowe, and T. Tomita, “High performance plasma amyloid-β biomarkers for Alzheimer’s disease,” Nature 554(7691), 249–254 (2018).
[Crossref]

Mashanovich, G. Z.

V. Mittal, M. Nedeljkovic, L. G. Carpenter, A. Z. Khokhar, H. M. H. Chong, G. Z. Mashanovich, P. N. Bartlett, and J. S. Wilkinson, “Waveguide absorption spectroscopy of bovine serum albumin in the mid-infrared fingerprint region,” ACS Sens. 4(7), 1749–1753 (2019).
[Crossref]

M. Nedeljkovic, J. S. Penades, V. Mittal, G. S. Murugan, A. Z. Khokhar, C. Littlejohns, L. G. Carpenter, C. B. Gawith, J. S. Wilkinson, and G. Z. Mashanovich, “Germanium-on-silicon waveguides operating at mid-infrared wavelengths up to 8.5 µm,” Opt. Express 25(22), 27431–27441 (2017).
[Crossref]

Millar, R. W.

Minor, W.

K. A. Majorek, P. J. Porebski, A. Dayal, M. D. Zimmerman, K. Jablonska, A. J. Stewart, M. Chruszcz, and W. Minor, “Structural and immunologic characterization of bovine, horse, and rabbit serum albumins,” Mol. Immunol. 52(3-4), 174–182 (2012).
[Crossref]

Mittal, V.

Mizaikoff, B.

Á. I. López-Lorente, P. Wang, M. Sieger, E. Vargas Catalan, M. Karlsson, F. Nikolajeff, L. Österlund, and B. Mizaikoff, “Mid-infrared thin-film diamond waveguides combined with tunable quantum cascade lasers for analyzing the secondary structure of proteins,” Phys. Status Solidi A 213(8), 2117–2123 (2016).
[Crossref]

M. Seiger and B. Mizaikoff, “Toward on-chip mid-infrared sensor,” Anal. Chem. 88(11), 5562–5573 (2016).
[Crossref]

R. Lu, W. W. Li, A. Katzir, Y. Raichlin, H. Q. Yu, and B. Mizaikoff, “Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors,” Analyst 140(3), 765–770 (2015).
[Crossref]

Mons, U.

A. Nabers, L. Perna, J. Lange, U. Mons, J. Schartner, J. Güldenhaupt, K. U. Saum, S. Janelidze, B. Holleczek, D. Rujescu, and O. Hansson, “Amyloid blood biomarker detects Alzheimer's disease,” EMBO Mol. Med. 10(5), 8763 (2018).
[Crossref]

Moorthy, B. S.

B. S. Moorthy, L. K. Iyer, and E. M. Topp, “Characterizing protein structure, dynamics and conformation in lyophilized solids,” Curr. Pharm. Des. 21(40), 5845–5853 (2015).
[Crossref]

Mudher, A.

G. Devitt, W. Rice, A. Crisford, I. Nandhakumar, A. Mudher, and S. Mahajan, “Conformational Evolution of Molecular Signatures during Amyloidogenic Protein Aggregation,” ACS Chem. Neurosci. 10(11), 4593–4611 (2019).
[Crossref]

G. Devitt, K. Howard, A. Mudher, and S. Mahajan, “Raman spectroscopy: an emerging tool in neurodegenerative disease research and diagnosis,” ACS Chem. Neurosci. 9(3), 404–420 (2018).
[Crossref]

Murugan, G. S.

Nabers, A.

A. Nabers, L. Perna, J. Lange, U. Mons, J. Schartner, J. Güldenhaupt, K. U. Saum, S. Janelidze, B. Holleczek, D. Rujescu, and O. Hansson, “Amyloid blood biomarker detects Alzheimer's disease,” EMBO Mol. Med. 10(5), 8763 (2018).
[Crossref]

Nakamura, A.

A. Nakamura, N. Kaneko, V. L. Villemagne, T. Kato, J. Doecke, V. Doré, C. Fowler, Q. X. Li, R. Martins, C. Rowe, and T. Tomita, “High performance plasma amyloid-β biomarkers for Alzheimer’s disease,” Nature 554(7691), 249–254 (2018).
[Crossref]

Nandhakumar, I.

G. Devitt, W. Rice, A. Crisford, I. Nandhakumar, A. Mudher, and S. Mahajan, “Conformational Evolution of Molecular Signatures during Amyloidogenic Protein Aggregation,” ACS Chem. Neurosci. 10(11), 4593–4611 (2019).
[Crossref]

Nedeljkovic, M.

Nikolajeff, F.

Á. I. López-Lorente, P. Wang, M. Sieger, E. Vargas Catalan, M. Karlsson, F. Nikolajeff, L. Österlund, and B. Mizaikoff, “Mid-infrared thin-film diamond waveguides combined with tunable quantum cascade lasers for analyzing the secondary structure of proteins,” Phys. Status Solidi A 213(8), 2117–2123 (2016).
[Crossref]

Odoli, C. O.

C. O. Odoli, P. Oduor-Odote, and S. Arason, “The influence of lipid content and pretreatment methods on protein conformation in fish (capelin, Mallotus villosus) during smoking and drying,” Food Sci. Nutr. 7(4), 1446–1454 (2019).
[Crossref]

Oduor-Odote, P.

C. O. Odoli, P. Oduor-Odote, and S. Arason, “The influence of lipid content and pretreatment methods on protein conformation in fish (capelin, Mallotus villosus) during smoking and drying,” Food Sci. Nutr. 7(4), 1446–1454 (2019).
[Crossref]

Orte, A.

N. Cremades, S. I. Cohen, E. Deas, A. Y. Abramov, A. Y. Chen, A. Orte, M. Sandal, R. W. Clarke, P. Dunne, F. A. Aprile, and C. W. Bertoncini, “Direct observation of the interconversion of normal and toxic forms of α-synuclein,” Cell 149(5), 1048–1059 (2012).
[Crossref]

Ortolani, M.

Österlund, L.

Á. I. López-Lorente, P. Wang, M. Sieger, E. Vargas Catalan, M. Karlsson, F. Nikolajeff, L. Österlund, and B. Mizaikoff, “Mid-infrared thin-film diamond waveguides combined with tunable quantum cascade lasers for analyzing the secondary structure of proteins,” Phys. Status Solidi A 213(8), 2117–2123 (2016).
[Crossref]

Paeder, V.

Paul, D. J.

Penades, J. S.

Perna, L.

A. Nabers, L. Perna, J. Lange, U. Mons, J. Schartner, J. Güldenhaupt, K. U. Saum, S. Janelidze, B. Holleczek, D. Rujescu, and O. Hansson, “Amyloid blood biomarker detects Alzheimer's disease,” EMBO Mol. Med. 10(5), 8763 (2018).
[Crossref]

Peters, J.

M. Tran, D. Huang, T. Komljenovic, J. Peters, A. Malik, and J. Bowers, “Ultra-low-loss silicon waveguides for heterogeneously integrated silicon/III-V photonics,” Appl. Sci. 8(7), 1139 (2018).
[Crossref]

Porebski, P. J.

K. A. Majorek, P. J. Porebski, A. Dayal, M. D. Zimmerman, K. Jablonska, A. J. Stewart, M. Chruszcz, and W. Minor, “Structural and immunologic characterization of bovine, horse, and rabbit serum albumins,” Mol. Immunol. 52(3-4), 174–182 (2012).
[Crossref]

Qiu, H. D.

W. Li, P. Anantha, K. H. Lee, H. D. Qiu, X. Guo, S. C. K. Goh, L. Zhang, H. Wang, R. A. Soref, and C. S. Tan, “Spiral waveguides on germanium-on-silicon nitride platform for mid-IR sensing applications,” IEEE Photonics J. 10(3), 1–7 (2018).
[Crossref]

Raichlin, Y.

R. Lu, W. W. Li, A. Katzir, Y. Raichlin, H. Q. Yu, and B. Mizaikoff, “Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors,” Analyst 140(3), 765–770 (2015).
[Crossref]

Rice, W.

G. Devitt, W. Rice, A. Crisford, I. Nandhakumar, A. Mudher, and S. Mahajan, “Conformational Evolution of Molecular Signatures during Amyloidogenic Protein Aggregation,” ACS Chem. Neurosci. 10(11), 4593–4611 (2019).
[Crossref]

Rinaldi, C.

D. Finlayson, C. Rinaldi, and M. J. Baker, “Is infrared spectroscopy ready for the clinic?” Anal. Chem. 91(19), 12117–12128 (2019).
[Crossref]

Rowe, C.

A. Nakamura, N. Kaneko, V. L. Villemagne, T. Kato, J. Doecke, V. Doré, C. Fowler, Q. X. Li, R. Martins, C. Rowe, and T. Tomita, “High performance plasma amyloid-β biomarkers for Alzheimer’s disease,” Nature 554(7691), 249–254 (2018).
[Crossref]

Rowe, D.

Rujescu, D.

A. Nabers, L. Perna, J. Lange, U. Mons, J. Schartner, J. Güldenhaupt, K. U. Saum, S. Janelidze, B. Holleczek, D. Rujescu, and O. Hansson, “Amyloid blood biomarker detects Alzheimer's disease,” EMBO Mol. Med. 10(5), 8763 (2018).
[Crossref]

Sandal, M.

N. Cremades, S. I. Cohen, E. Deas, A. Y. Abramov, A. Y. Chen, A. Orte, M. Sandal, R. W. Clarke, P. Dunne, F. A. Aprile, and C. W. Bertoncini, “Direct observation of the interconversion of normal and toxic forms of α-synuclein,” Cell 149(5), 1048–1059 (2012).
[Crossref]

Saum, K. U.

A. Nabers, L. Perna, J. Lange, U. Mons, J. Schartner, J. Güldenhaupt, K. U. Saum, S. Janelidze, B. Holleczek, D. Rujescu, and O. Hansson, “Amyloid blood biomarker detects Alzheimer's disease,” EMBO Mol. Med. 10(5), 8763 (2018).
[Crossref]

Schartner, J.

A. Nabers, L. Perna, J. Lange, U. Mons, J. Schartner, J. Güldenhaupt, K. U. Saum, S. Janelidze, B. Holleczek, D. Rujescu, and O. Hansson, “Amyloid blood biomarker detects Alzheimer's disease,” EMBO Mol. Med. 10(5), 8763 (2018).
[Crossref]

Scott, A. D.

J. Trevisan, P. P. Angelov, A. D. Scott, P. L. Carmichael, and F. L. Martin, “IRootLab: a free and open-source MATLAB toolbox for vibrational biospectroscopy data analysis,” Bioinformatics 29(8), 1095–1097 (2013).
[Crossref]

Seiger, M.

M. Seiger and B. Mizaikoff, “Toward on-chip mid-infrared sensor,” Anal. Chem. 88(11), 5562–5573 (2016).
[Crossref]

Sieger, M.

Á. I. López-Lorente, P. Wang, M. Sieger, E. Vargas Catalan, M. Karlsson, F. Nikolajeff, L. Österlund, and B. Mizaikoff, “Mid-infrared thin-film diamond waveguides combined with tunable quantum cascade lasers for analyzing the secondary structure of proteins,” Phys. Status Solidi A 213(8), 2117–2123 (2016).
[Crossref]

Smith, P. G.

Soref, R. A.

W. Li, P. Anantha, K. H. Lee, H. D. Qiu, X. Guo, S. C. K. Goh, L. Zhang, H. Wang, R. A. Soref, and C. S. Tan, “Spiral waveguides on germanium-on-silicon nitride platform for mid-IR sensing applications,” IEEE Photonics J. 10(3), 1–7 (2018).
[Crossref]

Sorel, M.

Stewart, A. J.

K. A. Majorek, P. J. Porebski, A. Dayal, M. D. Zimmerman, K. Jablonska, A. J. Stewart, M. Chruszcz, and W. Minor, “Structural and immunologic characterization of bovine, horse, and rabbit serum albumins,” Mol. Immunol. 52(3-4), 174–182 (2012).
[Crossref]

Tan, C. S.

W. Li, P. Anantha, K. H. Lee, H. D. Qiu, X. Guo, S. C. K. Goh, L. Zhang, H. Wang, R. A. Soref, and C. S. Tan, “Spiral waveguides on germanium-on-silicon nitride platform for mid-IR sensing applications,” IEEE Photonics J. 10(3), 1–7 (2018).
[Crossref]

Taneja, V.

M. Verma, A. Vats, and V. Taneja, “Toxic species in amyloid disorders: Oligomers or mature fibrils,” Ann. Indian Acad. Neurol. 18(2), 138 (2015).
[Crossref]

Tiné, M. R.

V. Della Porta, E. Bramanti, B. Campanella, M. R. Tiné, and C. Duce, “Conformational analysis of bovine serum albumin adsorbed on halloysite nanotubes and kaolinite: A Fourier transform infrared spectroscopy study,” RSC Adv. 6(76), 72386–72398 (2016).
[Crossref]

Tomita, T.

A. Nakamura, N. Kaneko, V. L. Villemagne, T. Kato, J. Doecke, V. Doré, C. Fowler, Q. X. Li, R. Martins, C. Rowe, and T. Tomita, “High performance plasma amyloid-β biomarkers for Alzheimer’s disease,” Nature 554(7691), 249–254 (2018).
[Crossref]

Topp, E. M.

B. S. Moorthy, L. K. Iyer, and E. M. Topp, “Characterizing protein structure, dynamics and conformation in lyophilized solids,” Curr. Pharm. Des. 21(40), 5845–5853 (2015).
[Crossref]

Tran, M.

M. Tran, D. Huang, T. Komljenovic, J. Peters, A. Malik, and J. Bowers, “Ultra-low-loss silicon waveguides for heterogeneously integrated silicon/III-V photonics,” Appl. Sci. 8(7), 1139 (2018).
[Crossref]

Trevisan, J.

J. Trevisan, P. P. Angelov, A. D. Scott, P. L. Carmichael, and F. L. Martin, “IRootLab: a free and open-source MATLAB toolbox for vibrational biospectroscopy data analysis,” Bioinformatics 29(8), 1095–1097 (2013).
[Crossref]

Vargas Catalan, E.

Á. I. López-Lorente, P. Wang, M. Sieger, E. Vargas Catalan, M. Karlsson, F. Nikolajeff, L. Österlund, and B. Mizaikoff, “Mid-infrared thin-film diamond waveguides combined with tunable quantum cascade lasers for analyzing the secondary structure of proteins,” Phys. Status Solidi A 213(8), 2117–2123 (2016).
[Crossref]

Vats, A.

M. Verma, A. Vats, and V. Taneja, “Toxic species in amyloid disorders: Oligomers or mature fibrils,” Ann. Indian Acad. Neurol. 18(2), 138 (2015).
[Crossref]

Verma, M.

M. Verma, A. Vats, and V. Taneja, “Toxic species in amyloid disorders: Oligomers or mature fibrils,” Ann. Indian Acad. Neurol. 18(2), 138 (2015).
[Crossref]

Villemagne, V. L.

A. Nakamura, N. Kaneko, V. L. Villemagne, T. Kato, J. Doecke, V. Doré, C. Fowler, Q. X. Li, R. Martins, C. Rowe, and T. Tomita, “High performance plasma amyloid-β biomarkers for Alzheimer’s disease,” Nature 554(7691), 249–254 (2018).
[Crossref]

Wang, H.

W. Li, P. Anantha, K. H. Lee, H. D. Qiu, X. Guo, S. C. K. Goh, L. Zhang, H. Wang, R. A. Soref, and C. S. Tan, “Spiral waveguides on germanium-on-silicon nitride platform for mid-IR sensing applications,” IEEE Photonics J. 10(3), 1–7 (2018).
[Crossref]

Wang, P.

Á. I. López-Lorente, P. Wang, M. Sieger, E. Vargas Catalan, M. Karlsson, F. Nikolajeff, L. Österlund, and B. Mizaikoff, “Mid-infrared thin-film diamond waveguides combined with tunable quantum cascade lasers for analyzing the secondary structure of proteins,” Phys. Status Solidi A 213(8), 2117–2123 (2016).
[Crossref]

Wilkinson, J. S.

Yu, H. Q.

R. Lu, W. W. Li, A. Katzir, Y. Raichlin, H. Q. Yu, and B. Mizaikoff, “Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors,” Analyst 140(3), 765–770 (2015).
[Crossref]

Zhang, L.

W. Li, P. Anantha, K. H. Lee, H. D. Qiu, X. Guo, S. C. K. Goh, L. Zhang, H. Wang, R. A. Soref, and C. S. Tan, “Spiral waveguides on germanium-on-silicon nitride platform for mid-IR sensing applications,” IEEE Photonics J. 10(3), 1–7 (2018).
[Crossref]

Zimmerman, M. D.

K. A. Majorek, P. J. Porebski, A. Dayal, M. D. Zimmerman, K. Jablonska, A. J. Stewart, M. Chruszcz, and W. Minor, “Structural and immunologic characterization of bovine, horse, and rabbit serum albumins,” Mol. Immunol. 52(3-4), 174–182 (2012).
[Crossref]

ACS Chem. Neurosci. (2)

G. Devitt, W. Rice, A. Crisford, I. Nandhakumar, A. Mudher, and S. Mahajan, “Conformational Evolution of Molecular Signatures during Amyloidogenic Protein Aggregation,” ACS Chem. Neurosci. 10(11), 4593–4611 (2019).
[Crossref]

G. Devitt, K. Howard, A. Mudher, and S. Mahajan, “Raman spectroscopy: an emerging tool in neurodegenerative disease research and diagnosis,” ACS Chem. Neurosci. 9(3), 404–420 (2018).
[Crossref]

ACS Sens. (1)

V. Mittal, M. Nedeljkovic, L. G. Carpenter, A. Z. Khokhar, H. M. H. Chong, G. Z. Mashanovich, P. N. Bartlett, and J. S. Wilkinson, “Waveguide absorption spectroscopy of bovine serum albumin in the mid-infrared fingerprint region,” ACS Sens. 4(7), 1749–1753 (2019).
[Crossref]

Adv. Protein Chem. (1)

S. Krimm and J. Bandekar, “Vibrational spectroscopy and conformation of peptides, polypeptides and proteins,” Adv. Protein Chem. 38, 181–364, Academic Press (1986).
[Crossref]

Anal. Chem. (2)

D. Finlayson, C. Rinaldi, and M. J. Baker, “Is infrared spectroscopy ready for the clinic?” Anal. Chem. 91(19), 12117–12128 (2019).
[Crossref]

M. Seiger and B. Mizaikoff, “Toward on-chip mid-infrared sensor,” Anal. Chem. 88(11), 5562–5573 (2016).
[Crossref]

Analyst (1)

R. Lu, W. W. Li, A. Katzir, Y. Raichlin, H. Q. Yu, and B. Mizaikoff, “Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors,” Analyst 140(3), 765–770 (2015).
[Crossref]

Ann. Indian Acad. Neurol. (1)

M. Verma, A. Vats, and V. Taneja, “Toxic species in amyloid disorders: Oligomers or mature fibrils,” Ann. Indian Acad. Neurol. 18(2), 138 (2015).
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Supplementary Material (1)

NameDescription
» Supplement 1       Principal component analysis of BSA monomer, oligomer and fibril amide I spectra.

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Figures (4)

Fig. 1.
Fig. 1. a) Schematic of the experimental apparatus (The cross-section of the waveguide is magnified), b) Photograph of the apparatus showing liquid from the pipette is introduced on the tail of the filter paper placed on GOS waveguide and c) IR image of cross-section of the GOS waveguide channel showing confinement of light.
Fig. 2.
Fig. 2. AFM images of (a) monomers and (b) oligomers and c) fibrils of BSA protein of area 1 µm x 1 µm. and height 15 nm.
Fig. 3.
Fig. 3. Waveguide absorption spectra of aqueous BSA solution measured on Ge on Si waveguide showing the amide I and II bands for monomers, oligomers and fibrils.
Fig. 4.
Fig. 4. Principal component analysis of BSA monomer and oligomer amide I spectra. a) 2-dimensional PCA scores plot showing distribution of monomer spectra (red diamonds) and oligomer spectra (blue diamonds) across PC1 and PC2 axes. b) PC1 loadings spectrum highlights the variation responsible for PCA scores.

Tables (1)

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Table 1. Assignment of deconvolved components of the amide I band 16-20