Abstract
It is well established that amyloid proteins play a primary role in neurodegenerative diseases. Alzheimer’s, Parkinson’s, type II diabetes, and Creutzfeldt-Jakob’s diseases are part of a wider family encompassing more than 50 human pathologies related to aggregation of proteins. Although this field of research is thoroughly investigated, several aspects of fibrillization remain misunderstood, which in turn slows down, or even impedes, advances in treating and curing amyloidoses. To solve this problem, several research groups have chosen to focus on short fragments of amyloid proteins, sequences that have been found to be of great importance for the amyloid formation process. Studying short peptides allows bypassing the complexity of working with full-length proteins and may provide important information relative to critical segments of amyloid proteins. To this end, efficient biophysical tools are required. In this review, we focus on two essential types of spectroscopic techniques, i.e., vibrational spectroscopy and its derivatives (conventional Raman scattering, deep-UV resonance Raman (DUVRR), Raman optical activity (ROA), surface-enhanced Raman spectroscopy (SERS), tip-enhanced Raman spectroscopy (TERS), infrared (IR) absorption spectroscopy, vibrational circular dichroism (VCD)) and solid-state nuclear magnetic resonance (ssNMR). These techniques revealed powerful to provide a better atomic and molecular comprehension of the amyloidogenic process and fibril structure. This review aims at underlining the information that these techniques can provide and at highlighting their strengths and weaknesses when studying amyloid fragments. Meaningful examples from the literature are provided for each technique, and their complementarity is stressed for the kinetic and structural characterization of amyloid fibril formation.
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Abbreviations
- 2D-IR:
-
Two-dimensional infrared
- 3D zf-TEDOR:
-
Three-dimensional z-filtered transferred-echo double-resonance
- A:
-
Absorbance
- AD:
-
Alzheimer’s disease
- AFM:
-
Atomic force microscopy
- AS:
-
α-Synuclein
- ATR-IR:
-
Attenuated total reflection infrared
- Aβ:
-
Amyloid-β
- Cryo-EM:
-
Cryo-electron microscopy
- CSA:
-
Chemical shift anisotropy
- DARR:
-
Dipolar-assisted rotational resonance
- DFT:
-
Density functional theory
- DNP:
-
Dynamic nuclear polarization
- DQF-DRAWS:
-
Double-quantum filtered dipolar recoupling in a windowless sequence
- DRAWS:
-
Dipolar recoupling in a windowless sequence
- DUVRR:
-
Deep-UV resonance Raman
- HD:
-
Huntington’s disease
- IAPP:
-
Islet amyloid polypeptide
- IR:
-
Infrared
- MAS:
-
Magic-angle spinning
- PD:
-
Parkinson’s disease
- PITHIRDS:
-
Constant-time recoupling with π-pulses lasting one-third of the MAS rotation period
- PolyQ:
-
Polyglutamine
- PPII:
-
Polyproline II helix
- PrP:
-
Prion protein
- R2 :
-
Rotational resonance
- REDOR:
-
Rotational-echo double-resonance
- ROA:
-
Raman optical activity
- SEM:
-
Scanning electron microscopy
- SERS:
-
Surface-enhanced Raman spectroscopy
- ssNMR:
-
Solid-state nuclear magnetic resonance
- STEM:
-
Scanning transmission electron microscopy
- STM:
-
Scanning tunneling microscopy
- TDC:
-
Transition dipole coupling
- TEDOR:
-
Transferred-echo double-resonance
- TEM:
-
Transmission electron microscopy
- TERS:
-
Tip-enhanced Raman spectroscopy
- TTR:
-
Transthyretin
- VCD:
-
Vibrational circular dichroism
- XRD:
-
X-ray diffraction
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Funding
The authors would like to acknowledge funding from the Natural Sciences and Engineering Research Council of Canada (NSERC), the Fonds de recherche du Québec - Nature et Technologies (FRQNT), the Regroupement québécois de recherche sur la fonction, l’ingénierie et les applications des protéines (PROTEO), the Centre de recherche sur les matériaux avancés (CERMA) and the Centre québécois sur les matériaux fonctionnels (CQMF). B.M. would like to acknowledge graduate scholarships from Bionano (NSERC) and PROTEO.
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Benjamin Martial declares that he has no conflict of interest. Thierry Lefèvre declares that he has no conflict of interest. Michèle Auger declares that she has no conflict of interest.
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Martial, B., Lefèvre, T. & Auger, M. Understanding amyloid fibril formation using protein fragments: structural investigations via vibrational spectroscopy and solid-state NMR. Biophys Rev 10, 1133–1149 (2018). https://doi.org/10.1007/s12551-018-0427-2
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DOI: https://doi.org/10.1007/s12551-018-0427-2