Literature DB >> 23746423

ATR-FTIR: a "rejuvenated" tool to investigate amyloid proteins.

Rabia Sarroukh1, Erik Goormaghtigh, Jean-Marie Ruysschaert, Vincent Raussens.   

Abstract

Amyloid refers to insoluble protein aggregates that are responsible for amyloid diseases but are also implicated in important physiological functions (functional amyloids). The widespread presence of protein aggregates but also, in most of the cases, their deleterious effects explain worldwide efforts made to understand their formation, structure and biological functions. We emphasized the role of FTIR and especially ATR-FTIR techniques in amyloid protein and/or peptide studies. The multiple advantages provided by ATR-FTIR allow an almost continuous structural view of protein/peptide conversion during the aggregation process. Moreover, it is now well-established that infrared can differentiate oligomers from fibrils simply on their spectral features. ATR-FTIR is certainly the fastest and easiest method to obtain this information. ATR-FTIR occupies a key position in the analysis and comprehension of the complex aggregation mechanism(s) at the oligomer and/or fibril level. These mechanism(s) seem to present strong similarities between different amyloid proteins and might therefore be extremely important to understand for both disease-associated and functional amyloid proteins. This article is part of a Special Issue entitled: FTIR in membrane proteins and peptide studies.
Copyright © 2013 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  8-anilino-1-naphthalenesulfonic acid; AD; ADDLs; ANS; ATR; Aggregate; Alzheimer's disease; Amyloid; Amyloid beta; Attenuated total reflection; Attenuated total reflection (ATR); Aβ; CD; EM; EPR; FTIR; Fourier-transform infrared spectroscopy; HETs; IAPP; IRE; Islet Amyloid Polypeptide; Oligomer; PrP; PrP(C); PrP(Sc); SDS-PAGE; SH3 domain; Sodium dodecyl sulfate polyacrylamide gel electrophoresis; Src homology 3 domain; TTR; ThT; Thioflavine T; Transthyretin; WB; Western Blot; amyloid-beta derived diffusible ligands; cellular prion protein; circular dichroism; electron microscopy; electron paramagnetic resonance; hIAPP; human Islet Amyloid Polypeptide; internal reflection element; pathological (scrapie) isoform of the prion protein; prion of the filamentous fungus P. anserine; prion protein; solid-state Nuclear magnetic resonance; ssNMR; β-sheet

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Year:  2013        PMID: 23746423     DOI: 10.1016/j.bbamem.2013.04.012

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  83 in total

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Review 3.  Understanding amyloid fibril formation using protein fragments: structural investigations via vibrational spectroscopy and solid-state NMR.

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Journal:  Biophys Rev       Date:  2018-05-31

4.  Optimization and partial characterization of intracellular anticandidal protein from Aspergillus giganteus MTCC 8408 using taguchi DOE.

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5.  Heterotropic Modulation of Amylin Fibrillation by Small Molecules: Implications for Formulative Designs.

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6.  Phosphorylation at Ser8 as an Intrinsic Regulatory Switch to Regulate the Morphologies and Structures of Alzheimer's 40-residue β-Amyloid (Aβ40) Fibrils.

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Journal:  J Biol Chem       Date:  2016-12-28       Impact factor: 5.157

7.  Effects of small-molecule amyloid modulators on a Drosophila model of Parkinson's disease.

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Review 8.  Biomolecular Assemblies: Moving from Observation to Predictive Design.

Authors:  Corey J Wilson; Andreas S Bommarius; Julie A Champion; Yury O Chernoff; David G Lynn; Anant K Paravastu; Chen Liang; Ming-Chien Hsieh; Jennifer M Heemstra
Journal:  Chem Rev       Date:  2018-10-03       Impact factor: 60.622

9.  Possible Existence of α-Sheets in the Amyloid Fibrils Formed by a TTR105-115 Mutant.

Authors:  Mary Rose Hilaire; Bei Ding; Debopreeti Mukherjee; Jianxin Chen; Feng Gai
Journal:  J Am Chem Soc       Date:  2018-01-04       Impact factor: 15.419

10.  Insights into the Aggregation Mechanism of PolyQ Proteins with Different Glutamine Repeat Lengths.

Authors:  Tetyana Yushchenko; Elke Deuerling; Karin Hauser
Journal:  Biophys J       Date:  2018-04-24       Impact factor: 4.033

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