Microscopic mechanism of protein cryopreservation in an aqueous solution with trehalose

Corradini, Dario; Strekalova, Elena G.; Stanley, H. Eugene; Gallo, Paola

doi:10.1038/srep01218

Cited by 129 publications

(130 citation statements)

References 62 publications

(100 reference statements)

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“…This possibly leads to its superior cryo-and lyoprotective properties [130]. MD simulations have been also performed in ternary LSZsugar-water systems at various sugar concentration [131][132][133][134]. More recently, a simulation of a solid state system composed by several LSZ proteins embedded in a low water glassy trehalose matrix has shown the presence of a more tight molecular packing of the proteins, which impairs the formation of large voids present in the dry LSZ glass without sugar [46].…”

Section: Atomistic Levelmentioning

confidence: 99%

Proteins in Saccharides Matrices and the Trehalose Peculiarity: Biochemical and Biophysical Properties

Cordone¹,

Cupane²,

Emanuele

et al. 2015

COC

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Immobilization of proteins and other biomolecules in saccharide matrices leads to a series of peculiar properties that are relevant from the point of view of both biochemistry and biophysics, and have important implications on related fields such as food industry, pharmaceutics, and medicine. In the last years, the properties of biomolecules embedded into glassy matrices and/or highly concentrated solutions of saccharides have been thoroughly investigated, at the molecular level, through in vivo, in vitro, and in silico studies. These systems show an outstanding ability to protect biostructures against stress conditions; various mechanisms appear to be at the basis of such bioprotection, that in the case of some sugars (in particular trehalose) is peculiarly effective.Here we review recent results obtained in our and other laboratories on ternary protein-sugar-water systems that have been typically studied in wide ranges of water content and temperature. Data from a large set of complementary experimental techniques provide a consistent description of structural, dynamical and functional properties of these systems, from atomistic to thermodynamic level.In the emerging picture, the stabilizing effect induced on the encapsulated systems might be attributed to a strong biomolecule-matrix coupling, mediated by extended hydrogen-bond networks, whose specific properties are determined by the saccharide composition and structure, and depend on water content.

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Section: Atomistic Levelmentioning

confidence: 99%

Proteins in Saccharides Matrices and the Trehalose Peculiarity: Biochemical and Biophysical Properties

Cordone¹,

Cupane²,

Emanuele

et al. 2015

COC

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“…The p = 1 bar isobar has been simulated on the 300 K-200 K temperature range. Further computational details can be found in [73,74]. Hydration water has been defined by the following criterio: each water molecules lying at a distance minor than or equal to 6 Å from any protein atoms.…”

Section: Methodsmentioning

confidence: 99%

“…At a given temperature the long temporal evolution of the SISF, differently from the free-water confined in MCM-41 pore, can not be reliably described by one relaxational process, but two different structural processes are needed to reproduce the long time behavior of such curves [73]. Consequently two structural relaxation times can be extracted from the SISFs.…”

Section: Protein Hydration Watermentioning

confidence: 99%

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Slow Dynamics and Structure of Supercooled Water in Confinement

Camisasca

Marzio

Rovere

et al. 2017

Entropy

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Abstract:We review our simulation results on properties of supercooled confined water. We consider two situations: water confined in a hydrophilic pore that mimics an MCM-41 environment and water at interface with a protein. The behavior upon cooling of the α relaxation of water in both environments is well interpreted in terms of the Mode Coupling Theory of glassy dynamics. Moreover, we find a crossover from a fragile to a strong regime. We relate this crossover to the crossing of the Widom line emanating from the liquid-liquid critical point, and in confinement we connect this crossover also to a crossover of the two body excess entropy of water upon cooling. Hydration water exhibits a second, distinctly slower relaxation caused by its dynamical coupling with the protein.The crossover upon cooling of this long relaxation is related to the protein dynamics.

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“…The stabilization of the protein native structure was believed to be enhanced by the reduced electrostatic solvation properties of the water layer towards the protein in the presence of trehalose (Lins et al, 2004). Corradini et al (2013) found that trehalose entraps water at the protein interface by forming a transient structure described as a cage. They observed that the dynamics of water in the layers close to the protein is significantly slower when trehalose is present in aqueous solutions of lysozyme and concluded that this slow water keeps the protein hydrated and inhibits crystallization.…”

Section: Mechanisms Of Bioprotectionmentioning

confidence: 99%