Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: a review

Kurouski, Dmitry; Duyne, Richard P. Van; Lednev, Igor K.

doi:10.1039/c5an00342c

Cited by 229 publications

(219 citation statements)

References 108 publications

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“…Unique bands were not observed, only varying intensities, with the exception of the calcite bands at the leading edge (region II) 31. The position of the Amide I bands in regions I–IV (1667 cm) corresponds to β‐sheets,32 and agrees with previous in situ infrared spectroscopy of the adhesive interface 33. Tables show vibrational band assignments,34 and intensity ratios ( N = 3; mean ± 95% confidence interval).…”

supporting

confidence: 86%

Acorn Barnacles Secrete Phase‐Separating Fluid to Clear Surfaces Ahead of Cement Deposition

et al. 2018

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Marine macrofoulers (e.g., barnacles, tubeworms, mussels) create underwater adhesives capable of attaching themselves to almost any material. The difficulty in removing these organisms frustrates maritime and oceanographic communities, and fascinates biomedical and industrial communities seeking synthetic adhesives that cure and hold steadfast in aqueous environments. Protein analysis can reveal the chemical composition of natural adhesives; however, developing synthetic analogs that mimic their performance remains a challenge due to an incomplete understanding of adhesion processes. Here, it is shown that acorn barnacles (Amphibalanus (=Balanus) amphitrite) secrete a phase‐separating fluid ahead of growth and cement deposition. This mixture consists of a phenolic laden gelatinous phase that presents a phase rich in lipids and reactive oxygen species at the seawater interface. Nearby biofilms rapidly oxidize and lift off the surface as the secretion advances. While phenolic chemistries are ubiquitous to arthropod adhesives and cuticles, the findings demonstrate that A. amphitrite uses these chemistries in a complex surface‐cleaning fluid, at a substantially higher relative abundance than in its adhesive. The discovery of this critical step in underwater adhesion represents a missing link between natural and synthetic adhesives, and provides new directions for the development of environmentally friendly biofouling solutions.

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confidence: 86%

Acorn Barnacles Secrete Phase‐Separating Fluid to Clear Surfaces Ahead of Cement Deposition

et al. 2018

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“…Deep UV resonance Raman spectroscopy (DUVRR) is a powerful tool for structural characterization of aggregated proteins and peptides [29]. The sensitivity of the amide M A N U S C R I P T A C C E P T E D ACCEPTED MANUSCRIPT 8 chromophore Raman signature to Ψ dihedral angle makes this technique uniquely capable of differentiating between globular and fibrillar β-sheet conformations and between parallel and antiparallel β-sheets [19,30].…”

Section: Formation Of Acrylodan-labeledmentioning

confidence: 99%

Structural differences between amyloid beta oligomers

Breydo

Kurouski

Rasool

et al. 2016

Biochemical and Biophysical Research Communications

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“…This so-called polymorphism can be investigated by scanning electron microscopy (SEM) or atomic force microscopy (AFM)61011. Another common feature of amyloid fibrils is a highly organized hydrogen bonded β-sheet structure core, which is detectable in the bulk sample with various techniques, including solid-state nuclear magnetic resonance (NMR)2, X-ray diffraction2, vibrational circular dichroism12, infrared spectroscopy13, and Raman spectroscopy1415. Single-particle studies on the nanoscale with tip-enhanced Raman scattering (TERS) on insulin fibrils161718 and human islet amyloid precursor peptide (hIAPP) fibrils19 revealed that the surface is not only composed of β-sheet structures but also has a high propensity for α-helix/unordered structures.…”

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confidence: 99%

High resolution spectroscopy reveals fibrillation inhibition pathways of insulin

Deckert‐Gaudig

Deckert

2016

Sci Rep

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Fibril formation implies the conversion of a protein’s native secondary structure and is associated with several neurodegenerative diseases. A better understanding of fibrillation inhibition and fibril dissection requires nanoscale molecular characterization of amyloid structures involved. Tip-enhanced Raman scattering (TERS) has already been used to chemically analyze amyloid fibrils on a sub-protein unit basis. Here, TERS in combination with atomic force microscopy (AFM), and conventional Raman spectroscopy characterizes insulin assemblies generated during inhibition and dissection experiments in the presence of benzonitrile, dimethylsulfoxide, quercetin, and β-carotene. The AFM topography indicates formation of filamentous or bead-like insulin self-assemblies. Information on the secondary structure of bulk samples and of single aggregates is obtained from standard Raman and TERS measurements. In particular the high spatial resolution of TERS reveals the surface conformations associated with the specific agents. The insulin aggregates formed under different inhibition and dissection conditions can show a similar morphology but differ in their β-sheet structure content. This suggests different aggregation pathways where the prevention of the β-sheet stacking of the peptide chains plays a major role. The presented approach is not limited to amyloid-related reasearch but can be readily applied to systems requiring extremely surface-sensitive characterization without the need of labels.

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Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: a review

Cited by 229 publications

References 108 publications

Acorn Barnacles Secrete Phase‐Separating Fluid to Clear Surfaces Ahead of Cement Deposition

Acorn Barnacles Secrete Phase‐Separating Fluid to Clear Surfaces Ahead of Cement Deposition

Structural differences between amyloid beta oligomers

High resolution spectroscopy reveals fibrillation inhibition pathways of insulin

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