Systematic Analysis of Aggregates from 38 Kinds of Non Disease-Related Proteins: Identifying the Intrinsic Propensity of Polypeptides to Form Amyloid Fibrils

Aso, Yoshikazu; Shiraki, Kentaro; Takagi, Masahiro

doi:10.1271/bbb.60718

Cited by 37 publications

(33 citation statements)

References 47 publications

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“…Some fragments were more truncated and contained only residues 1-17, 1-18, 120-129 or an additional cleavage between residues 18 and 19 [80]. Similar fragments in fibrils and HEWL solutions have been observed by other groups [96,122,126]. The difference observed between the fragments in the fibril and resulting solution led to the hypothesis that either fragmentation occurs first followed by the selective aggregation of one fragment and/or that full-length HEWL forms fibrils and is subsequently cleaved [80]; a model proposed by Mishra et al supports both pathways [96].…”

Section: Chemical Modifications Of Hewl At Low Ph and Elevated Tempersupporting

confidence: 74%

The Formation of Amyloid Fibrils from Proteins in the Lysozyme Family

Trexler¹,

Nilsson²

2007

CPPS

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Amyloid fibrils are highly ordered protein assemblies known to contribute to the pathology of a variety of genetic and aging-associated diseases. More recently, these fibrils have been shown to be useful as structural scaffolds in both natural biological systems and nanotechnology applications. The intense interest in amyloid fibrils has led to the investigation of well-characterized proteins, such as hen egg white lysozyme (HEWL), as model systems to examine structural and mechanistic principles that may be generally applicable to all amyloid fibrils. The purpose of this review is to critically examine the fibril-formation literature of proteins in the lysozyme family with respect to the known structure and folding properties of these proteins. The goal is to identify similarities and differences within the family, examine general misfolding / aggregation principles, and identify key areas of importance for future work on the fibril formation of these proteins.

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Section: Chemical Modifications Of Hewl At Low Ph and Elevated Tempersupporting

confidence: 74%

The Formation of Amyloid Fibrils from Proteins in the Lysozyme Family

Trexler¹,

Nilsson²

2007

CPPS

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“…These proteins form an oligomer or intermediate after becoming unfolded, aggregated and finally limbless amyloid-like fibrils [8,9], which are toxic in most but not all cases. This complicated situation has stimulated research into the causal link between amyloid fibrils and disease [10,11]. Amyloid beta peptide (Aβ), associated with the cause of Alzheimer's disease, was shown to be cytotoxic, and it was reported that its early aggregations (oligomers) as well as its prefibrillar aggregates have stronger cytotoxicity than the mature fibrils themselves [12].…”

Section: Introductionmentioning

confidence: 99%

Amyloidogenic lysozymes accumulate in the endoplasmic reticulum accompanied by the augmentation of ER stress signals

Kamada

Kusakabe

Sugimoto

2015

Biochimica et Biophysica Acta (BBA) - General Subjects

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“…The pH dependence of the thermal unfolding of H2A-H2B and H3-H4 has been reported, although at lower ionic strengths. 41,42 Between pH 4.5 and 5.5, the mid-point of the thermal unfolding transition, T M , for the H3-H4 heterodimer was [50][51][52][53][54][55][56][57][58][59][60] C, depending on the protein concentration, while the T M of H2A-H2B was 10-15 C lower. Thus, H3-H4 is more stable, but forms fibrils much more readily than H2A-H2B or the individual H2A and H2B monomers which are only partially folded even under stabilizing conditions.…”

Section: Fibrillation Propensity Of Different Histonesmentioning

confidence: 99%

The impact of solubility and electrostatics on fibril formation by the H3 and H4 histones

Topping

Gloss

2011

Protein Science

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The goal of this study was to examine fibril formation by the heterodimeric eukaryotic histones (H2A-H2B and H3-H4) and homodimeric archaeal histones (hMfB and hPyA1). The histone fold dimerization motif is an obligatorily domain-swapped structure comprised of two fused helix:b-loop:helix motifs. Domain swapping has been proposed as a mechanism for the evolution of protein oligomers as well as a means to form precursors in the formation of amyloid-like fibrils. Despite sharing a common fold, the eukaryotic histones of the core nucleosome and archaeal histones fold by kinetic mechanisms of differing complexity with transient population of partially folded monomeric and/or dimeric species. No relationship was apparent between fibrillation propensity and equilibrium stability or population of kinetic intermediates. Only H3 and H4, as isolated monomers and as a heterodimer, readily formed fibrils at room temperature, and this propensity correlates with the significantly lower solubility of these polypeptides. The fibrils were characterized by ThT fluorescence, FTIR, and far-UV CD spectroscopies and electron microscopy. The helical histone fold comprises the protease-resistant core of the fibrils, with little or no protease protection of the poorly structured N-terminal tails. The highly charged tails inhibit fibrillation through electrostatic repulsion. Kinetic studies indicate that H3 and H4 form a co-fibril, with simultaneous incorporation of both histones. The potential impact of H3 and H4 fibrillation on the cytotoxicity of extracellular histones and a-synuclein-mediated neurotoxicity and fibrillation is considered.

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Systematic Analysis of Aggregates from 38 Kinds of Non Disease-Related Proteins: Identifying the Intrinsic Propensity of Polypeptides to Form Amyloid Fibrils

Cited by 37 publications

References 47 publications

The Formation of Amyloid Fibrils from Proteins in the Lysozyme Family

The Formation of Amyloid Fibrils from Proteins in the Lysozyme Family

Amyloidogenic lysozymes accumulate in the endoplasmic reticulum accompanied by the augmentation of ER stress signals

The impact of solubility and electrostatics on fibril formation by the H3 and H4 histones

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