160
G. Compagnini et al.
46. S.A. Hudson, T. Ecroyd, W. Kee et al., The thioflavin T fluorescence assay for amyloid fibril
detection can be biased by the presence of exogenous compounds. FEBS 276, 5960–5972
(2009)
47. R.N. Rambaran, L.C. Serpell, Amyloid fibrils. Prion 2, 112–117 (2008)
48. M. Pannuzzo, D. Milardi, A. Raudino et al., Analytical model and multiscale simulations of
Aβ peptide aggregation in lipid membranes: towards a unifying description of conformational
transitions, oligomerization and membrane damage. Phys. Chem. Chem. Phys. 15, 8940–8951
(2013)
49. V. Amendola, M. Meneghetti, S. Fiameni et al., SERS labels for quantitative assays: application
to the quantification of gold nanoparticles uptaken by macrophage cells. Anal. Methods 3,
849–856 (2011)
50. G. Grasso, L. D’Urso, E. Messina et al., A mass spectrometry and surface enhanced Raman
spectroscopy study of the interaction between linear carbon chains and noble metals. Carbon
47, 2611–2619 (2009)
51. I. ChoiYun, S. Huh, D. Erickson et al., Ultra-sensitive, label-free probing of the conformational
characteristics of amyloid beta aggregates with a SERS active nanofluidic device. Microfluid.
Nanofluid. 1, 663–669 (2012)
52. D. Bhowmik, K.R. Mote, C.M. MacLaughlin et al., Cell-membrane-mimicking lipid-coated
nanoparticles confer Raman enhancement to membrane proteins and reveal membrane-attached
amyloid-β conformation. ACS Nano 9, 9070–9077 (2015)
53. D. Kurouski, T. Deckert-Gaudig, V. Deckert et al., Surface characterization of insulin protofilaments and fibril polymorphs using tip-enhanced Raman spectroscopy (TERS). Biophys. J.
106, 263–271 (2014)
54. D. Zhang, O. Neumann, H. Wang, V.M. Yuwono et al., Gold nanoparticles can induce the
formation of protein-based aggregates at physiological pH. Nano Lett. 9, 666–671 (2009)
55. Y. Liao, Y. Chang, Y. Yoshiike et al., Negatively charged gold nanoparticles inhibit Alzheimer’s
amyloid-β fibrillization, induce fibril dissociation, and mitigate neurotoxicity. Small 8, 3631–
3639 (2012)
56. G. Brancolini, A. Corazza, M. Vuano et al., Probing the influence of citrate-capped gold
nanoparticles on an amyloidogenic protein. ACS Nano 9, 2600–2613 (2015)
57. C. Rehbock, J. Jakobi, L. Gamrad et al., Current state of laser synthesis of metal and alloy
nanoparticles as ligand-free reference materials for nano-toxicological assays. J. Nanotechnol.
5, 1523–1541 (2014)
58. W.H. Moore, S. Krimm, Vibrational analysis of peptides, polypeptides, and proteins. II. βpoly(L-alanine) and β-poly(L-alanylglycine). Biopolymers 15, 2465–2483 (1976)
59. W.L. Peticolas, Applications of Raman spectroscopy to biological macromolecules. Biochimie
57(4), 417–428 (1975)
60. B.G. Frushour, P.C. Painter, J.L. Koenig, Vibrational spectra of polypeptides. J. Macromol.
Chem. 15, 29–115 (1976)
61. T.G. Spiro, B.P. Gaber, Laser Raman scattering as a probe of protein structure. Annu. Rev.
Biochem. 46, 553–572 (1977)
62. J.F. Rabolt, W.H. Moore, S. Krimm, Vibrational analysis of peptides, polypeptides, and proteins.
3. alpha-poly(L-alanine). Macromolecules 10, 1065–1074 (1977)
63. J. Bandekar, S. Krimmt, Vibrational analysis of peptides, polypeptides, and proteins: characteristic amide bands of β-turns. Biophysics 76, 774–777 (1979)
64. C. Cabaleiro-Lago, F. Quinlan-Pluck, I. Lynch et al., Inhibition of amyloid β protein fibrillation
by polymeric nanoparticles. J. Am. Chem. Soc. 130, 15437–15443 (2008)
65. L. D’Urso, M. Condorelli, O. Puglisi et al., Detection and characterization at nM concentration
of oligomers formed by hIAPP, Aβ(1–40) and their equimolar mixture using SERS and MD
simulations. Phys. Chem. Chem. Phys. 20, 20588–20596 (2018)
66. A. Mendez, F. Fernandez, G. Gasco, Removal of malachite green using carbon-based
adsorbents. Desalination 206, 147–153 (2007)
67. M.Z. Iqbal, A.A. Abdala, Thermally reduced graphene: synthesis, characterization and dye
removal applications. RSC Adv. 3, 24455–24464 (2013)
G. Compagnini et al.
46. S.A. Hudson, T. Ecroyd, W. Kee et al., The thioflavin T fluorescence assay for amyloid fibril
detection can be biased by the presence of exogenous compounds. FEBS 276, 5960–5972
(2009)
47. R.N. Rambaran, L.C. Serpell, Amyloid fibrils. Prion 2, 112–117 (2008)
48. M. Pannuzzo, D. Milardi, A. Raudino et al., Analytical model and multiscale simulations of
Aβ peptide aggregation in lipid membranes: towards a unifying description of conformational
transitions, oligomerization and membrane damage. Phys. Chem. Chem. Phys. 15, 8940–8951
(2013)
49. V. Amendola, M. Meneghetti, S. Fiameni et al., SERS labels for quantitative assays: application
to the quantification of gold nanoparticles uptaken by macrophage cells. Anal. Methods 3,
849–856 (2011)
50. G. Grasso, L. D’Urso, E. Messina et al., A mass spectrometry and surface enhanced Raman
spectroscopy study of the interaction between linear carbon chains and noble metals. Carbon
47, 2611–2619 (2009)
51. I. ChoiYun, S. Huh, D. Erickson et al., Ultra-sensitive, label-free probing of the conformational
characteristics of amyloid beta aggregates with a SERS active nanofluidic device. Microfluid.
Nanofluid. 1, 663–669 (2012)
52. D. Bhowmik, K.R. Mote, C.M. MacLaughlin et al., Cell-membrane-mimicking lipid-coated
nanoparticles confer Raman enhancement to membrane proteins and reveal membrane-attached
amyloid-β conformation. ACS Nano 9, 9070–9077 (2015)
53. D. Kurouski, T. Deckert-Gaudig, V. Deckert et al., Surface characterization of insulin protofilaments and fibril polymorphs using tip-enhanced Raman spectroscopy (TERS). Biophys. J.
106, 263–271 (2014)
54. D. Zhang, O. Neumann, H. Wang, V.M. Yuwono et al., Gold nanoparticles can induce the
formation of protein-based aggregates at physiological pH. Nano Lett. 9, 666–671 (2009)
55. Y. Liao, Y. Chang, Y. Yoshiike et al., Negatively charged gold nanoparticles inhibit Alzheimer’s
amyloid-β fibrillization, induce fibril dissociation, and mitigate neurotoxicity. Small 8, 3631–
3639 (2012)
56. G. Brancolini, A. Corazza, M. Vuano et al., Probing the influence of citrate-capped gold
nanoparticles on an amyloidogenic protein. ACS Nano 9, 2600–2613 (2015)
57. C. Rehbock, J. Jakobi, L. Gamrad et al., Current state of laser synthesis of metal and alloy
nanoparticles as ligand-free reference materials for nano-toxicological assays. J. Nanotechnol.
5, 1523–1541 (2014)
58. W.H. Moore, S. Krimm, Vibrational analysis of peptides, polypeptides, and proteins. II. βpoly(L-alanine) and β-poly(L-alanylglycine). Biopolymers 15, 2465–2483 (1976)
59. W.L. Peticolas, Applications of Raman spectroscopy to biological macromolecules. Biochimie
57(4), 417–428 (1975)
60. B.G. Frushour, P.C. Painter, J.L. Koenig, Vibrational spectra of polypeptides. J. Macromol.
Chem. 15, 29–115 (1976)
61. T.G. Spiro, B.P. Gaber, Laser Raman scattering as a probe of protein structure. Annu. Rev.
Biochem. 46, 553–572 (1977)
62. J.F. Rabolt, W.H. Moore, S. Krimm, Vibrational analysis of peptides, polypeptides, and proteins.
3. alpha-poly(L-alanine). Macromolecules 10, 1065–1074 (1977)
63. J. Bandekar, S. Krimmt, Vibrational analysis of peptides, polypeptides, and proteins: characteristic amide bands of β-turns. Biophysics 76, 774–777 (1979)
64. C. Cabaleiro-Lago, F. Quinlan-Pluck, I. Lynch et al., Inhibition of amyloid β protein fibrillation
by polymeric nanoparticles. J. Am. Chem. Soc. 130, 15437–15443 (2008)
65. L. D’Urso, M. Condorelli, O. Puglisi et al., Detection and characterization at nM concentration
of oligomers formed by hIAPP, Aβ(1–40) and their equimolar mixture using SERS and MD
simulations. Phys. Chem. Chem. Phys. 20, 20588–20596 (2018)
66. A. Mendez, F. Fernandez, G. Gasco, Removal of malachite green using carbon-based
adsorbents. Desalination 206, 147–153 (2007)
67. M.Z. Iqbal, A.A. Abdala, Thermally reduced graphene: synthesis, characterization and dye
removal applications. RSC Adv. 3, 24455–24464 (2013)