Cold‐ and Pressure‐Induced Dissociation of Protein Aggregates and Amyloid Fibrils

Mishra, Rajesh; Winter, Roland

doi:10.1002/anie.200802027

Cited by 113 publications

(117 citation statements)

References 24 publications

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“…The formation of oligomers and amyloid fibrils is influenced by a broad range of features of the physicochemical environment, including temperature, 134 pressure, 135 pH value, 36 buffer system, 136 organic cosolvents, 137 detergents, 138 ionic strength and general ion composition of a sample. 139,140 In addition, the oligomerization reactions can be affected by small molecules, proteins and amyloid secondary compounds, such as lipids, 141 glycosaminoglycanes 142 and serum amyloid P component.…”

Section: Effectors Of Oligomer Formation and Oligomer-specific Inhibimentioning

confidence: 99%

Oligomeric Intermediates in Amyloid Formation: Structure Determination and Mechanisms of Toxicity

Fändrich

2012

Journal of Molecular Biology

310

312

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Section: Effectors Of Oligomer Formation and Oligomer-specific Inhibimentioning

confidence: 99%

Oligomeric Intermediates in Amyloid Formation: Structure Determination and Mechanisms of Toxicity

Fändrich

2012

Journal of Molecular Biology

310

312

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“…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%

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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“…It is experimentally known that the amyloid fibrils are dissociated into monomers when a high pressure is applied to the system [7][8][9]. We discuss this experimental observation using Equation (10).…”

Section: Comment On Formation/dissociation Process Of Amyloid Fibrilsmentioning

confidence: 95%

“…It has been observed in experiments that denaturation of the native structure (pressure denaturation) [2][3][4][5][6] and dissolution of amyloid-fibrils [7][8][9] and virus assemblies [10] occur at high pressures. A common feature of these phenomena is that the volume change upon the pressure denaturation and dissociation is negative [3,6,10,11].…”

Section: Introductionmentioning

confidence: 99%

“…A common feature of these phenomena is that the volume change upon the pressure denaturation and dissociation is negative [3,6,10,11]. These pressure effects have often been discussed in terms of the Le Châtelier principle, which states that a pressure increase will shift a given equilibrium to the side that occupies the smallest volume [3,6,9]. Although this discussion is simple, the microscopic mechanism of pressure effects on the structures formed by biological self-assembly processes is still unclear.…”

Section: Introductionmentioning

confidence: 99%

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General Framework of Pressure Effects on Structures Formed by Entropically Driven Self-Assembly

Yoshidome

2010

Entropy

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Abstract:We review a general framework of pressure effects on the structures formed by entropically driven self-assembly (for example, denaturation of proteins from their native structure and dissociation of ordered structure of the amyloid fibril occur at high pressures). In the framework, the translational entropy of water is an essential factor. Our findings are as follows: at low pressures, the structures almost minimizing the excluded volume (EV) generated for water molecules are stable. On the other hand, at high pressures, the structures possessing the largest possible water-accessible surface area together with sufficiently small EV become more stable. These characteristics are consistent with experimental observations.

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Cold‐ and Pressure‐Induced Dissociation of Protein Aggregates and Amyloid Fibrils

Cited by 113 publications

References 24 publications

Oligomeric Intermediates in Amyloid Formation: Structure Determination and Mechanisms of Toxicity

Oligomeric Intermediates in Amyloid Formation: Structure Determination and Mechanisms of Toxicity

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

General Framework of Pressure Effects on Structures Formed by Entropically Driven Self-Assembly

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