Stepwise Organization of the β-Structure Identifies Key Regions Essential for the Propagation and Cytotoxicity of Insulin Amyloid Fibrils

Chatani, Eri; Imamura, Hiroshi; Yamamoto, Naoki; Kato, Masaru

doi:10.1074/jbc.m113.520874

Cited by 60 publications

(71 citation statements)

References 60 publications

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“…Amyloid aggregation of insulin was studied by incubating the monomer samples (~40 μM) in 10 mM PBS at ~70 °C in the presence and in the absence of AuNPs Tyr , AuNPs Trp , and AgNPs Tyr nanoparticles (Mark et al 2004;Chatani et al 2014). Small aliquots of these aggregating samples were taken out at regular intervals and their Thioflavin T fluorescence intensities were recorded.…”

Section: Amyloid Aggregation Of Insulinmentioning

confidence: 99%

Tyrosine- and tryptophan-coated gold nanoparticles inhibit amyloid aggregation of insulin

et al. 2015

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Here, we have strategically synthesized stable gold (AuNPs(Tyr), AuNPs(Trp)) and silver (AgNPs(Tyr)) nanoparticles which are surface functionalized with either tyrosine or tryptophan residues and have examined their potential to inhibit amyloid aggregation of insulin. Inhibition of both spontaneous and seed-induced aggregation of insulin was observed in the presence of AuNPs(Tyr), AgNPs(Tyr), and AuNPs(Trp) nanoparticles. These nanoparticles also triggered the disassembly of insulin amyloid fibrils. Surface functionalization of amino acids appears to be important for the inhibition effect since isolated tryptophan and tyrosine molecules did not prevent insulin aggregation. Bioinformatics analysis predicts involvement of tyrosine in H-bonding interactions mediated by its C=O, -NH2, and aromatic moiety. These results offer significant opportunities for developing nanoparticle-based therapeutics against diseases related to protein aggregation.

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Section: Amyloid Aggregation Of Insulinmentioning

confidence: 99%

Tyrosine- and tryptophan-coated gold nanoparticles inhibit amyloid aggregation of insulin

et al. 2015

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“…18 The effects of chemical denaturation, pH, temperature and pressure on the structural stability of insulin and its amyloids have been studied previously. [19][20][21][22][23][24] Insulin amyloid is used as the model amyloid because this amyloid forms in a structure (the parallel intermolecular β-sheet structure) similar to that of toxic amyloids such as α-synuclein related to the neurodegenerative diseases. 19,[23][24][25] Moreover, insulin amyloid aggregate is related to the injection-localized amyloidosis.…”

Section: Introductionmentioning

confidence: 99%

“…26 Insulin easily forms amyloid aggregates under acidic pH and high temperature. 21,23 Amyloid formations, such as myoglobin, lysozyme, ribonuclease A, and cytochrome c, were also prepared in vitro under conditions of extreme pH and high temperature. [27][28][29][30] These proteins and insulin in vitro are similarly amyloidogenic.…”

Section: Introductionmentioning

confidence: 99%

Suppression Effect on the Formation of Insulin Amyloid by the Use of Ionic Liquids

Takekiyo

Yamaguchi

Abe

et al. 2015

ACS Sustainable Chem. Eng.

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Using congo red assay and Fourier transform infrared spectroscopy, we have investigated the suppression of bovine insulin amyloid formation by the addition of 1-butyl-3-methylimidazolium thiocyanate ([bmim][SCN]), ethylammonium nitrate ([EAN][NO 3 ]), and propylammonium nitrate ([PAN][NO 3 ]) ionic liquids (ILs). The results of our investigations showed that the three studied ILs strongly inhibit the formation of insulin amyloid. Furthermore, the condensed solutions containing [EAN][NO 3 ] and [PAN][NO 3 ] demonstrated a higher protectant ability for the structure of monomeric insulin rather than that of [bmim] [SCN]. To investigate the mechanism underlying the suppression ability of ILs, the interaction site of ILs and amino acid residues in insulin was determined. The affinity between ILs and specific amino acid residues in insulin was found to be the main cause for the suppression of insulin amyloid formation. The present finding is that ILs can be potentially used as the suppression agent of insulin amyloid aggregates.

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“…[1] Amyloid nucleation is started from misfolded and unfolded conformations of proteins and leads to fibrillation through mutual interactions of prefibrillar oligomer intermediates. [2] Protein crystallization is coupled with the formation of protein clusters containing solvent waters and the subsequent generation of ah ighly concentrated area of such clusters. [3] Nucleation and the crystal growth proceed in such an area of af ew tens to af ew hundreds of nanometers.M ost of the experiments for amyloid formation and crystallization are carried out in solution by tuning pH, [1] salt concentration, [1] and temperature [2] and by applying ultrasonication, [3] electro-magnetic field, [4] and pulsed laser irradiation.…”

mentioning

confidence: 99%

A Single Spherical Assembly of Protein Amyloid Fibrils Formed by Laser Trapping

et al. 2017

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Protein amyloids have received much attention owing to their correlation with serious diseases and to their promising mechanical and optical properties as future materials. Amyloid formation has been conducted by tuning temperature and chemical conditions, so that its nucleation and the following growth are analyzed as ensemble dynamics. A single spherical assembly of amyloid fibrils of cytochrome c domain‐swapped dimer was successfully generated upon laser trapping. The amyloid fibrillar structure was confirmed by fluorescence characterization and electron microscopy. The prepared spheres were further manipulated individually in solution to fabricate a three‐dimensional microstructure and a line pattern. Amyloid formation dynamics and amyloid‐based microstructure fabrication are demonstrated based on direct observation of a single spherical assembly, which foresees a new approach in amyloid studies.

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Stepwise Organization of the β-Structure Identifies Key Regions Essential for the Propagation and Cytotoxicity of Insulin Amyloid Fibrils

Cited by 60 publications

References 60 publications

Tyrosine- and tryptophan-coated gold nanoparticles inhibit amyloid aggregation of insulin

Tyrosine- and tryptophan-coated gold nanoparticles inhibit amyloid aggregation of insulin

Suppression Effect on the Formation of Insulin Amyloid by the Use of Ionic Liquids

A Single Spherical Assembly of Protein Amyloid Fibrils Formed by Laser Trapping

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