Amyloid fibril formation <i>in vitro</i> from halophilic metal binding protein: Its high solubility and reversibility minimized formation of amorphous protein aggregations

Tokunaga, Yuhei; Matsumoto, Mitsuharu; Tokunaga, Masao; Arakawa, Tsutomu; Sugimoto, Yasushi

doi:10.1002/pro.2359

Cited by 3 publications

(3 citation statements)

References 44 publications

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“…It had been an open question as to how exactly do these three core regions participate in fibril formation. An example where a single core peptide region among several potential core regions was able to form fibrils was also observed for His-tagged halophilic protein (62). Various details, such as the precise ratio of the core peptides incorporated into the finished fibrils, as well as the order of interaction of each peptide within the fibrils, remain to be determined.…”

Section: Identification Of Core Peptides and Its Fibrillationmentioning

confidence: 99%

Structural basis of Cu, Zn-superoxide dismutase amyloid fibril formation involves interaction of multiple peptide core regions

Ida¹,

Ando²,

Adachi³

et al. 2015

J Biochem

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Cu, Zn-superoxide dismutase (SOD1), an enzyme implicated in the progression of familial amyotrophic lateral sclerosis (fALS), forms amyloid fibrils under certain experimental conditions. As part of our efforts to understand ALS pathogenesis, in this study we found that reduction of the intramolecular disulfide bond destabilized the tertiary structure of metal free wildtype SOD1 and greatly enhanced fibril formation in vitro. We also identified fibril core peptides that are resistant to protease digestion by using mass spectroscopy and Edman degradation analyses. Three regions dispersed throughout the sequence were detected as fibril core sequences of SOD1. Interestingly, by using three synthetic peptides that correspond to these identified regions, we determined that each region was capable of fibril formation, either alone or in a mixture containing multiple peptides. It was also revealed that by reducing the disulfide bond and causing a decrease in the structural stability, the amyloid fibril formation of a familial mutant SOD1 G93A was accelerated even under physiological conditions. These results demonstrate that by destabilizing the structure of SOD1 by removing metal ions and breaking the intramolecular disulfide bridge, multiple fibril-forming core regions are exposed, which then interact with each another and form amyloid fibrils under physiological conditions.

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Section: Identification Of Core Peptides and Its Fibrillationmentioning

confidence: 99%

Structural basis of Cu, Zn-superoxide dismutase amyloid fibril formation involves interaction of multiple peptide core regions

Ida¹,

Ando²,

Adachi³

et al. 2015

J Biochem

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“…Amyloid fibrils are a well-known type of peptide/protein-based nanostructure. , They are defined as having a “cross-β” structure, in which β-strands run perpendicular to the long axis of the fibril . Some forms of amyloid are soluble, while others are not. , Amyloids can be prepared from either proteins or peptides. ,, Examples include the self-assembly of a prion determinant from yeast and the self-assembly of a diphenylalanine peptide that is the core recognition motif of Alzheimer’s β-amyloid peptide. ,, The synthesis of amyloid fibrils generally requires harsh conditions for proteins that are not naturally amyloidogenic. Insulin amyloid fibrils form at very high temperatures (∼100 °C), while lysozyme amyloid fibrils form under acidic conditions. , Once formed, amyloid fibrils are generally resistant to stress such as heat, organic solvents, and proteases. − …”

mentioning

confidence: 99%

“…9 Some forms of amyloid are soluble, while others are not. 10,11 Amyloids can be prepared from either proteins or peptides. 9,12,13 Examples include the self-assembly of a prion determinant from yeast 13 and the self-assembly of a diphenylalanine peptide that is the core recognition motif of Alzheimer's β-amyloid peptide.…”

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confidence: 99%

Extraordinarily Stable Amyloid Fibrils Engineered from Structurally Defined β-Solenoid Proteins

2017

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The self-assembly of biological molecules into ordered nanostructures is an attractive method for fabricating novel nanomaterials. Nucleic acid-based nanostructures suffer from limitations to functionalization and stability. Alternatively, protein-based nanostructures have advantageous chemical properties, but design facility lags behind that of nucleic acids. Structurally defined fibrils engineered from β-solenoid proteins (BSPs) form under mild conditions [Peralta, M. D. R., et al. (2015) ACS Nano 9, 449-463] and are good candidates for novel nanomaterials because of the defined sequence-to-structure relationship and tunable properties. Here, the stability of two types of engineered fibrils was examined using circular dichroism spectroscopy, transmission electron microscopy, and electrophoresis. Both are stable to at least 90 °C, and one survives autoclaving. They are stable toward organic solvents, urea, and pH extremes. One is even stable in 2% sodium dodecyl sulfate with heating. The fibrils show variable resistance to proteolytic digestion: one is resistant to trypsin, but chymotrypsin and proteinase K degrade both. These results show that BSPs have excellent potential for bottom-up design of rugged, functional, amyloid-based nanomaterials.

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Rapid enrichment of peptides with calcium-chelating capacity and characterization of physical chemical properties

Wang

et al. 2019

Acta Alimentaria

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Casein peptides with calcium-chelating capacity were rapidly enriched by using a novel ceramic matrix (CM)-based Ti4+-IMAC adsorbent. The ability of calcium-chelating peptides (CCPs) to bind calcium and the physical properties of complexes formed between CCPs and calcium were investigated. Results demonstrated that the amount of calcium bound depended on the degree of hydrolysis (DH) of casein hydrolysates. The highest calcium binding capacity (683 mg g−1) occurred when bovine casein was hydrolysed by pancreatin at a DH of 0.14%, meanwhile, the calcium content of CCPs-Ca complex exhibited the maximum level (134.96 mg g−1). In addition, CCPs showed a higher radical scavenging capacity (50 µg ml−1; 99% inhibition, or an equivalent activity of 9.91×10−3 M Trolox) compared to casein digest. Moreover, Fourier-transform infrared spectroscopy and fluorescence spectroscopy were used to explore the interaction between CPPs and calcium, and the results demonstrated that phosphoserine residues as well as COO- groups of CCPs were involved in the formation of CCPs-Ca complex.

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Amyloid fibril formation in vitro from halophilic metal binding protein: Its high solubility and reversibility minimized formation of amorphous protein aggregations

Cited by 3 publications

References 44 publications

Structural basis of Cu, Zn-superoxide dismutase amyloid fibril formation involves interaction of multiple peptide core regions

Structural basis of Cu, Zn-superoxide dismutase amyloid fibril formation involves interaction of multiple peptide core regions

Extraordinarily Stable Amyloid Fibrils Engineered from Structurally Defined β-Solenoid Proteins

Rapid enrichment of peptides with calcium-chelating capacity and characterization of physical chemical properties

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