High-Pressure Chemical Biology and Biotechnology

Silva, Jerson L.; Oliveira, Andréa C.; Vieira, Tuane C. R. G.; Oliveira, Guilherme A. P. de; Suarez, Marisa C.; Foguel, Débora

doi:10.1021/cr400204z

Cited by 192 publications

(223 citation statements)

References 260 publications

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“…Similar effects www.chemphyschem.org have been observed for the effect of pressure on the stability of multimeric proteins and amyloid forming polypeptides. [37][38][39][40][41][42] TMAO is an atural compatible osmolyte, which is in particular found in stressed organisms, and acts as protein stabilizer and "chemical chaperon". [26][27][28]43] The addition of 1 m TMAO (Figure 2b)t ot he actin solution leads to as ignificant increase of the polymerization reaction.…”

Section: Resultsmentioning

confidence: 99%

Combined Effects of Temperature, Pressure, and Co‐Solvents on the Polymerization Kinetics of Actin

et al. 2015

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In vivo studies have shown that the cytoskeleton of cells is very sensitive to changes in temperature and pressure. In particular, actin filaments get depolymerized when pressure is increased up to several hundred bars, conditions that are easily encountered in the deep sea. We quantitatively evaluate the effects of temperature, pressure, and osmolytes on the kinetics of the polymerization reaction of actin by high-pressure stopped-flow experiments in combination with fluorescence detection and an integrative stochastic simulation of the polymerization process. We show that the compatible osmolyte trimethylamine-N-oxide is not only able to compensate for the strongly retarding effect of chaotropic agents, such as urea, on actin polymerization, it is also able to largely offset the deteriorating effect of pressure on actin polymerization, thereby allowing biological cells to better cope with extreme environmental conditions.

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Section: Resultsmentioning

confidence: 99%

Combined Effects of Temperature, Pressure, and Co‐Solvents on the Polymerization Kinetics of Actin

et al. 2015

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“…Although both chemical and pressure denaturation processes are controlled by Le Chatelier's principle, the molecular mechanisms are different. We know that pressure shifts the equilibrium toward the denatured state due to the negative volume change, which is generally explained by a combination of several effects: the disruption of water-excluded cavities in the protein interior, electrostriction of broken salt bridges, and general water solvation (10)(11)(12)(13)(14). Monitoring each amino acid residue by NMR has permitted us to map the progressive effects of pressure.…”

Section: Discussionmentioning

confidence: 99%

“…Much debate regarding the contributions of cavities and hydration to the negative volume change upon unfolding, as well as compressibility effects, exists (10)(11)(12)(13)(14). Using NMR, the "squeezing" of the hydrogen bonds in parallel with the heterogeneous release of the water-excluded cavities by hydration was explored.…”

Section: Discussionmentioning

confidence: 99%

“…Currently, pressure is extensively used in various biological and biotechnological applications (10)(11)(12)(13) and is one of the most promising variables enabling the structural analysis of these protein substates. The application of pressure to a protein forces the water shell into the protein, thus shifting the equilibrium of the system from the native state to an intermediate or to the unfolded state.…”

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confidence: 99%

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A hypothesis to reconcile the physical and chemical unfolding of proteins

Oliveira

Silva

2015

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

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High pressure (HP) or urea is commonly used to disturb folding species. Pressure favors the reversible unfolding of proteins by causing changes in the volumetric properties of the protein-solvent system. However, no mechanistic model has fully elucidated the effects of urea on structure unfolding, even though proteinurea interactions are considered to be crucial. Here, we provide NMR spectroscopy and 3D reconstructions from X-ray scattering to develop the "push-and-pull" hypothesis, which helps to explain the initial mechanism of chemical unfolding in light of the physical events triggered by HP. In studying MpNep2 from Moniliophthora perniciosa, we tracked two cooperative units using HP-NMR as MpNep2 moved uphill in the energy landscape; this process contrasts with the overall structural unfolding that occurs upon reaching a threshold concentration of urea. At subdenaturing concentrations of urea, we were able to trap a state in which urea is preferentially bound to the protein (as determined by NMR intensities and chemical shifts); this state is still folded and not additionally exposed to solvent [fluorescence and small-angle X-ray scattering (SAXS)]. This state has a higher susceptibility to pressure denaturation (lower p 1/2 and larger ΔV u ); thus, urea and HP share concomitant effects of urea binding and pulling and water-inducing pushing, respectively. These observations explain the differences between the molecular mechanisms that control the physical and chemical unfolding of proteins, thus opening up new possibilities for the study of protein folding and providing an interpretation of the nature of cooperativity in the folding and unfolding processes.protein folding | hydrostatic pressure | urea | NMR | SAXS

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“…The difference between the expected behavior and the one resulting from SAXS data analysis can be ascribed to the evidence that, similarly to folded proteins, fibrillar aggregates have packing defects that modify their answer to pressure. Hence, the decrease of the average fibril radius with pressure and the simultaneous increase of their electron densities, can be considered the signature of a gradual disappearing of internal cavities, electrostriction of broken electrostatic interactions and additional hydration [62]. These results seem to confirm the existence of packing defects in the fibril core and the participation of hydrophobic interactions in their structure that make them responsive to moderate pressures.…”

Section: Saxsmentioning

confidence: 72%

Pressure effects on α-synuclein amyloid fibrils: An experimental investigation on their dissociation and reversible nature

Piccirilli

Plotegher

Spinozzi

et al. 2017

Archives of Biochemistry and Biophysics

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Abstractα-synuclein amyloid fibrils are found in surviving neurons of Parkinson's disease affected patients, but the role they play in the disease development is still under debate. A growing number of evidences point to soluble oligomers as the major cytotoxic species, while insoluble fibrillar aggregates could even play a protection role. In this work, we investigate α-synuclein fibrils dissociation induced at high pressure by means of Small Angle X-ray Scattering and Fourier Transform Infrared Spectroscopy. Fibrils were produced from wild type α-synuclein and two mutants associated with Parkinson's disease, A30P and A53T. Our results enlighten the different reversible nature of α-synuclein fibrils fragmentation at high pressure and suggest water excluded volumes presence in the fibrils core. Wild type and A30P species stabilized at high pressure are highly amyloidogenic and quickly re-associate into fibrils upon decompression, while A53T species shows a partial reversibility of the process likely due to the presence of an intermediate oligomeric state stabilized at high pressure. The amyloid fibrils dissociation process is here suggested to be associated to a negative activation volume, supporting the notion that α-synuclein fibrils are in a high-volume and high-compressibility state and hinting at the presence of a hydration-mediated activated state from which dissociation occurs.

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High-Pressure Chemical Biology and Biotechnology

Cited by 192 publications

References 260 publications

Combined Effects of Temperature, Pressure, and Co‐Solvents on the Polymerization Kinetics of Actin

Combined Effects of Temperature, Pressure, and Co‐Solvents on the Polymerization Kinetics of Actin

A hypothesis to reconcile the physical and chemical unfolding of proteins

Pressure effects on α-synuclein amyloid fibrils: An experimental investigation on their dissociation and reversible nature

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