pH-dependent disintegration of insulin amyloid fibrils monitored with atomic force microscopy and surface-enhanced Raman spectroscopy

Applications of Single-Molecule Vibrational Spectroscopic Techniques for the Structural Investigation of Amyloid Oligomers

“…TERS, in a similar fashion to AFM-IR, combines plasmon-enhanced Raman spectroscopy [ 48 ] with AFM. Already for a number of years, a wealth of work has been published on single-molecule TERS of amyloid fibrils [ 101 , 102 , 103 , 104 , 105 , 106 , 107 ]. We would like to highlight the work by Deckert-Gaudig et al [ 108 ], in which the hydrophobicity of insulin fibril subdomains was mapped and co-localized with amino acid TERS signatures at a high spatial resolution.…”

One- and Two-Photon Excited Autofluorescence of Lysozyme Amyloids

“… 1 − 4 Their formation can be accomplished under laboratory conditions at low pH and elevated temperatures. 2 , 5 One of their peculiar properties is the presence of a common backbone architecture, i.e., secondary β-sheet structure stabilized by a hydrogen-bonding (H-bonding) network. 3 , 6 , 7 Another interesting feature of amyloid structures is their intrinsic fluorescence.…”

“…The name amyloid refers to peptide or protein aggregates associated with certain neurodegenerative disorders including Parkinson’s disease, Alzheimer’s disease (AD), and type II diabetes. − Their formation can be accomplished under laboratory conditions at low pH and elevated temperatures. , One of their peculiar properties is the presence of a common backbone architecture, i.e., secondary β-sheet structure stabilized by a hydrogen-bonding (H-bonding) network. ,, Another interesting feature of amyloid structures is their intrinsic fluorescence. − Upon excitation at 350–380 nm, emission occurs in the visible range of spectrum, ca. 430–450 nm. ,, The exact mechanism of the phenomenon still remains elusive, with several hypotheses having been put forward.…”