Salt-induced formations of partially folded intermediates and amyloid fibrils suggests a common underlying mechanism

Goto, Yuji; Adachi, Masayuki; Muta, Hiroya; So, Masatomo

doi:10.1007/s12551-017-0370-7

Cited by 41 publications

(57 citation statements)

References 65 publications

(101 reference statements)

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“…Considering the presence of a large number of negatively charged phosphate groups, the marked effects of polyPs on the amyloid formation of β2m may be caused by the salt effects. Three major mechanisms generally participate in salt or ion effects on proteins (31,32).…”

Section: Discussionmentioning

confidence: 99%

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Possible mechanisms of polyphosphate-induced amyloid fibril formation of β ₂ -microglobulin

Zhang

Yamaguchi

et al. 2019

Proc. Natl. Acad. Sci. U.S.A.

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Polyphosphate (polyP), which is found in various microorganisms and human cells, is an anionic biopolymer consisting of inorganic phosphates linked by high-energy phosphate bonds. Previous studies revealed that polyPs strongly promoted the amyloid formation of several amyloidogenic proteins; however, the mechanism of polyP-induced amyloid formation remains unclear. In the present study using β 2 -microglobulin (β2m), a protein responsible for dialysisrelated amyloidosis, we investigated amyloid formation in the presence of various chain lengths of polyPs at different concentrations under both acidic (pH 2.0 to 2.5) and neutral pH (pH 7.0 to 7.5) conditions. We found that the amyloid formation of β2m at acidic pH was significantly accelerated by the addition of polyPs at an optimal polyP concentration, which decreased with an increase in chain length. The results obtained indicated that electrostatic interactions between positively charged β2m and negatively charged polyPs play a major role in amyloid formation. Under neutral pH conditions, long polyP with 60 to 70 phosphates induced the amyloid formation of β2m at several micromoles per liter, a similar concentration range to that in vivo. Since β2m with an isoelectric point of 6.4 has a slightly negative net charge at pH 7, polyPs were unlikely to interact with β2m electrostatically. PolyPs appear to dehydrate water molecules around β2m under the unfolded conformation, leading to the preferential stabilization of less water-exposed amyloid fibrils. These results not only revealed the pH-dependent mechanism of the amyloid formation of β2m but also suggested that polyPs play an important role in the development of dialysis-related amyloidosis.amyloid fibrillation | amorphous aggregation | dialysis-related amyloidosis | polyphosphates | supersaturation

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Section: Discussionmentioning

confidence: 99%

“…These three types of salt or ion effects on proteins may be distinguished from the concentration range and order of effectiveness of various salts or ions (31,32).…”

Section: Discussionmentioning

confidence: 99%

Possible mechanisms of polyphosphate-induced amyloid fibril formation of β ₂ -microglobulin

Zhang

Yamaguchi

et al. 2019

Proc. Natl. Acad. Sci. U.S.A.

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“…Only in some studies, the change in the α-helicity of the protein structure is recorded as a consequence of structural destabilization [28,29]. Thus, due to competing effects non-polar and polar solvation at protein surfaces, the detailed molecular mechanism of the effect of neutral salts on protein structures is still a subject of intense investigation [30]. Thus, the accumulation of experimental studies of particular protein-salt systems is needed to improve the theory.…”

Section: Introductionmentioning

confidence: 99%

FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts

et al. 2020

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The effect of neutral salts on protein conformation was first analyzed by Hofmeister in 1888, however, even today this phenomenon is not completely understood. To clarify this effect, we studied changes in the secondary structure of two proteins: human serum albumin with predominantly α-helical structure and porcine pancreas β-trypsin with the typical β-structural arrangement in aqueous solutions of neutral salts (KSCN, KCl, (NH4)2SO4). The changes in the secondary structure were studied at 23 °C and 80 °C by using the second derivative deconvolution method of the IR spectra. Our results demonstrated that the ability of the salts to stabilize/destabilize these two proteins correlates with the Hofmeister series of ions. At the same time, some exceptions were also observed. The destabilization of the native structures of both α-helical albumin and β-structural trypsin upon interaction with neutral salts leads to the formation of intermolecular β-sheets typical for amyloid fibrils or amorphous aggregates. Thus, our quantitative FTIR-spectroscopy analysis allowed us to further clarify the mechanisms and complexity of the neutral salt actions on protein structures which may lead to strategies preventing unwelcome misfolding of proteins.

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“…11). It is in honour of this service that we have contributions from a number of fellow APPA council members (North et al 2018;Tayo 2017;Sawitri et al 2018;Song 2018;Goto et al 2018).…”

Section: Scientific Process-societies and Servicementioning

confidence: 99%

Foreword to ‘Multiscale structural biology: biophysical principles and mechanisms underlying the action of bio-nanomachines’, a special issue in Honour of Fumio Arisaka’s 70th birthday

2018

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This issue of Biophysical Reviews, titled 'Multiscale structural biology: biophysical principles and mechanisms underlying the action of bio-nanomachines', is a collection of articles dedicated in honour of Professor Fumio Arisaka's 70th birthday. Initially, working in the fields of haemocyanin and actin filament assembly, Fumio went on to publish important work on the elucidation of structural and functional aspects of T4 phage biology. As his career has transitioned levels of complexity from proteins (hemocyanin) to large protein complexes (actin) to even more massive bio-nanomachinery (phage), it is fitting that the subject of this special issue is similarly reflective of his multiscale approach to structural biology. This festschrift contains articles spanning biophysical structure and function from the bio-molecular through to the bio-nanomachine level.

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Salt-induced formations of partially folded intermediates and amyloid fibrils suggests a common underlying mechanism

Cited by 41 publications

References 65 publications

Possible mechanisms of polyphosphate-induced amyloid fibril formation of β ₂ -microglobulin

Possible mechanisms of polyphosphate-induced amyloid fibril formation of β ₂ -microglobulin

FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts

Foreword to ‘Multiscale structural biology: biophysical principles and mechanisms underlying the action of bio-nanomachines’, a special issue in Honour of Fumio Arisaka’s 70th birthday

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Salt-induced formations of partially folded intermediates and amyloid fibrils suggests a common underlying mechanism

Cited by 41 publications

References 65 publications

Possible mechanisms of polyphosphate-induced amyloid fibril formation of β 2 -microglobulin

Possible mechanisms of polyphosphate-induced amyloid fibril formation of β 2 -microglobulin

FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts

Foreword to ‘Multiscale structural biology: biophysical principles and mechanisms underlying the action of bio-nanomachines’, a special issue in Honour of Fumio Arisaka’s 70th birthday

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Product

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Possible mechanisms of polyphosphate-induced amyloid fibril formation of β ₂ -microglobulin

Possible mechanisms of polyphosphate-induced amyloid fibril formation of β ₂ -microglobulin