Pressure-jump NMR Study of Dissociation and Association of Amyloid Protofibrils

Kamatari, Yuji O.; Yokoyama, Shigeyuki; Tachibana, Hideki; Akasaka, Kazuyuki

doi:10.1016/j.jmb.2005.04.010

Cited by 52 publications

(54 citation statements)

References 17 publications

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“…For proteins, these volume changes arise from contributions of internal cavities and interactions with hydration water (68). Our findings suggest that the packing defects and hydrophobic pockets in mature PrP fibrillar structures disappear upon pressure treatment and that the sum of the dissociated prion protein conformers and the new fibrillar species occupy a smaller volume than the initial amyloid fibrils, in agreement with previous volumetric measurements of amyloid fibrils (35,40,69,70). Moreover, several recent reports indicate the existence in amyloid fibrils of well defined ThT binding sites (71) that form cavities of about 8 -9 Å in diameter.…”

Section: Discussionsupporting

confidence: 90%

“…Dissociation of amyloid fibrils can be triggered by the addition of highly concentrated chemical denaturants such as urea or guanidinium hydrochloride or of trifluoroethanol and the use of high temperature (30 -34). Although not as well studied, the application of elevated pressure has also been used to dissociate non-mature amyloid fibrils and proto-fibrils of several proteins (35)(36)(37)(38)(39)(40)(41)(42).…”

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confidence: 99%

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Amyloid Features and Neuronal Toxicity of Mature Prion Fibrils Are Highly Sensitive to High Pressure

Moustaine

Perrier

et al. 2011

Journal of Biological Chemistry

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Prion proteins (PrP) can aggregate into toxic and possibly infectious amyloid fibrils. This particular macrostructure confers on them an extreme and still unexplained stability. To provide mechanistic insights into this self-assembly process, we used high pressure as a thermodynamic tool for perturbing the structure of mature amyloid fibrils that were prepared from recombinant full-length mouse PrP. Application of high pressure led to irreversible loss of several specific amyloid features, such as thioflavin T and 8-anilino-1-naphthalene sulfonate binding, alteration of the characteristic proteinase K digestion pattern, and a significant decrease in the ␤-sheet structure and cytotoxicity of amyloid fibrils. Partial disaggregation of the mature fibrils into monomeric soluble PrP was observed. The remaining amyloid fibrils underwent a change in secondary structure that led to morphologically different fibrils composed of a reduced number of proto-filaments. The kinetics of these reactions was studied by recording the pressure-induced dissociation of thioflavin T from the amyloid fibrils. Analysis of the pressure and temperature dependence of the relaxation rates revealed partly unstructured and hydrated kinetic transition states and highlighted the importance of collapsing and hydrating inter-and intramolecular cavities to overcome the high free energy barrier that stabilizes amyloid fibrils.Amyloid fibrils are filamentous polypeptide aggregates that are associated with devastating disorders such as Alzheimer and Parkinson diseases, type II diabetes, and prion (proteinaceous infectious particle) diseases, including Creutzfeldt-Jakob and mad cow disease (1, 2). There is increasing evidence that under appropriate conditions the amyloid state is accessible also to many other proteins that are not related to diseases, suggesting that the amyloid state is a generic structural feature, which might be adopted by any polypeptide chain (3-6).The development of in vitro model systems together with various biophysical and biochemical techniques (7-9) has improved the knowledge on the physicochemical basis of amyloid formation as well as on their structural and biochemical properties. It is now well recognized that a common property of amyloid fibrils is the extensive stacking of intermolecular ␤-strands that are arranged perpendicularly to the fibril axis and stabilized by a dense network of non-covalent interactions (10 -13). These fibrils consist of a variable number and arrangement of thin assemblies called proto-filaments that give rise to different fibril morphologies of diameters between 5 and 30 nanometers, both in in vitro preparations or in tissues (14 -22). Fibrils and their precursors are generally cytotoxic (23, 24) and are, thus, thought to be responsible for the neurodegeneration that is associated with many amyloid diseases.Yet the fundamental parameters that govern the protein aggregation process and dictate fibril stability/clearance are not well known. As the study of protein folding has been greatly advanc...

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Section: Discussionsupporting

confidence: 90%

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confidence: 99%

Amyloid Features and Neuronal Toxicity of Mature Prion Fibrils Are Highly Sensitive to High Pressure

Moustaine

Perrier

et al. 2011

Journal of Biological Chemistry

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“…4F), showing that the oligomerization is a spontaneous process as observed previously in amyloid protofibril formation. 13 However, compared to the original spectrum (Fig. 4C), the intensity of the broad component is still reduced and the signals assignable to monomeric huPrP C (23-231) have a higher intensity.…”

Section: Resultsmentioning

confidence: 84%

“…Pressurejump 1 H-NMR was used previously to monitor the dissociation and association reaction of amyloid protofibrils. 13 We apply here the same technique to monitor the dissociation and association reaction of prion oligomers. Figure 4D AGAAAAGA motif and S1-Loop-HelixA-Loop-S2-Loop-HelixC, are engaged in intra-and/or inter-molecular interactions.…”

Section: Resultsmentioning

confidence: 99%

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Reversible monomer-oligomer transition in human prion protein

Sasaki

Gaikwad

Hashiguchi

et al. 2008

Prion

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The structure and the dissociation reaction of oligomers PrP oligo from reduced human prion huPrP C (23-231) have been studied by 1 H-NMR and tryptophan fluorescence spectroscopy at varying pressure, along with circular dichroism and atomic force microscopy. The 1 H-NMR and fluorescence spectral feature of the oligomer is consistent with the notion that the N-terminal residues including all seven Trp residues, are free and mobile, while residues 105~210, comprising the AGAAAAGA motif and S1-Loop-HelixA-Loop-S2-Loop-HelixC, are engaged in intra-and/ or inter-molecular interactions. By increasing pressure to 200 MPa, the oligomers tend to dissociate into monomers which may be identified with PrP C* , a rare metastable form of PrP C stabilized at high pressure (Kachel et al., BMC Struct Biol 6:16). The results strongly suggest that the oligomeric form PrP oligo is in dynamic equilibrium with the monomeric forms via PrP C* , namely huPrP C  huPrP C*  huPrP oligo .

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High hydrostatic pressure effect on proteins: Fluorescence studies

Ando

Barstow

2012

Encyclopedia of Analytical Chemistry

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Life on Earth can survive and often thrive at pressures ranging from half atmospheric pressure to over 10 000 times atmospheric pressure. Despite this fact, the effects of pressure on biological systems remain relatively unexplored, particularly those on biological macromolecules. Fluorescence spectroscopy is a sensitive probe of the structural and chemical states of macromolecules and is the most widely available and affordable technique for the study of macromolecules under high pressure. When combined with structural techniques such as high‐pressure X‐ray crystallography and small‐angle X‐ray scattering (SAXS), fluorescence spectroscopy provides deep insights into the forces that bind proteins together and imbue them with function. In this article, we describe modern experimental techniques for high‐pressure fluorescence spectroscopy along with examples of their use in the study of the protein structure‐function relationship and protein unfolding under high pressure.

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Pressure-jump NMR Study of Dissociation and Association of Amyloid Protofibrils

Cited by 52 publications

References 17 publications

Amyloid Features and Neuronal Toxicity of Mature Prion Fibrils Are Highly Sensitive to High Pressure

Amyloid Features and Neuronal Toxicity of Mature Prion Fibrils Are Highly Sensitive to High Pressure

Reversible monomer-oligomer transition in human prion protein

High hydrostatic pressure effect on proteins: Fluorescence studies

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