Trehalose solution viscosity at low temperatures measured by dynamic light scattering method: Trehalose depresses molecular transportation for ice crystal growth

Uchida, Tsutomu; Nagayama, Masaichi; Gohara, Kazutoshi

doi:10.1016/j.jcrysgro.2009.09.023

Cited by 27 publications

(26 citation statements)

References 30 publications

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“…The extracted correlation times of s c = 130 ± 10 ps in water-sucrose and 160 ± 10 ps in watertrehalose give a slightly higher microscopic viscosity in trehalose. This is in agreement with the results of numerous studies of water-disaccharide solutions [95][96][97][98]. The difference between s c = 130 ps in the 50 % w/w water-sucrose solution and 1.2 ns in the rehydrated sucrose sample is reasonable considering the fact that the molar ratios of water/disaccharide are about 20 in the solution and 2.5 in the matrix, as determined by FTIR.…”

Section: W-band Epr Of Rehydrated Matricessupporting

confidence: 92%

The Magic of Disaccharide Glass Matrices for Protein Function as Decoded by High-Field EPR and FTIR Spectroscopy

et al. 2015

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The structural and dynamical interaction of proteins with their microenvironment in disordered matrices plays a decisive role for their function; EPR spectroscopy is a powerful tool for shading light onto the molecular mechanisms of this protein-matrix interplay. To clarify the molecular mechanisms of disaccharide bioprotection, we studied the structure and dynamics of spin-labeled systems and photosynthetic reaction centers (RCs) in sucrose and trehalose matrices at different hydration levels by means of cw and pulse high-field 95 GHz (W-band) EPR as well as by FTIR. In this minireview, we summarize and discuss EPR and FTIR experiments showing that the anhydrobiotic state of the RC-trehalose system (1) is not the result of matrix-induced changes of the local structure of the charge-separated radical-pair cofactors, P Áþ 865 and Q ÁÀ A , and (2) is not the result of changes of local dynamics and local hydrogen bonding of Q A in its binding pocket. Rather, the extreme impairment of RC dynamics caused by incorporation into the dehydrated trehalose matrix, which also protects it against thermal denaturation, originates in the high rigidity, already at room temperature, of the dry trehalose glass matrix coating the RC protein surface. This surface hydrogen-bonding scaffold shifts the correlation time of thermal conformational fluctuations into the non-biological time domain. Another intriguing aspect of disaccharide bioprotection is the superior The authors dedicate this work to Giovanni Giacometti on the occasion of his 85th birthday. AppliedMagnetic Resonance efficiency of trehalose versus sucrose matrices in stabilizing the anhydrobiotic state of proteins. To clarify the molecular basis of this specificity, glassy trehalose-water and sucrose-water binary systems, incorporating a nitroxide radical as spin probe, have been studied by high-field W-band EPR spectroscopy at different water contents. Analysis of the EPR spectra revealed a different structural and dynamical organization in the sucrose and trehalose matrix, only the trehalose being homogeneous in terms of residual water and nitroxide distribution.

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Section: W-band Epr Of Rehydrated Matricessupporting

confidence: 92%

The Magic of Disaccharide Glass Matrices for Protein Function as Decoded by High-Field EPR and FTIR Spectroscopy

et al. 2015

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“…For example it was reported that 1-10% w/w sucrose or trehalose solutions exhibited very similar rheological properties to those of pure water. 25 However, direct evidence on the differential hydrogen bonding of the evaluated cryoprotectant with Cit-GNPs is required to fully explain their differential cryoprotective ability and should be the subject of a subsequent study. 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 To follow the aggregation of GNPs quantitatively, two methods were employed: dynamic light scattering (DLS) and plasmon band broadening.…”

Section: Stability Of Citmentioning

confidence: 99%

Colloidal Stability of Citrate and Mercaptoacetic Acid Capped Gold Nanoparticles upon Lyophilization: Effect of Capping Ligand Attachment and Type of Cryoprotectants

et al. 2014

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For various applications of gold nanotechnology, long-term nanoparticle stability in solution is a major challenge. Lyophilization (freeze-drying) is a widely used process to convert labile protein and various colloidal systems into powder for improved long-term stability. However, the lyophilization process itself may induce various stresses resulting in nanoparticle aggregation. Despite a plethora of studies evaluating lyophilization of proteins, liposomes, and polymeric nanoparticles, little is known about the stability of gold nanoparticles (GNPs) upon lyophilization. Herein, the effects of lyophilization and freeze-thaw cycles on the stability of two types of GNPs: Citrate-capped GNPs (stabilized via weakly physisorbed citrate ions, Cit-GNPs) and mercaptoacetic acid-capped GNPs (stabilized via strongly chemisorbed mercaptoacetic acid, MAA-GNPs) are investigated. Both types of GNPs have similar core size and effective surface charge as evident from transmission electron microscopy and zeta potential measurements, respectively. Plasmon absorption of GNPs and its dependence on nanoparticle aggregation was employed to follow stability of GNPs in combination with dynamic light scattering analysis. Plasmon peak broadening index (PPBI) is proposed herein for the first time to quantify GNPs aggregation using nonlinear Gaussian fitting of GNPs UV-vis spectra. Our results indicate that Cit-GNPs aggregate irreversibly upon freeze-thaw cycles and lyophilization. In contrast, MAA-GNPs exhibits remarkable stability under the same conditions. Cit-GNPs exhibit no significant aggregation in the presence of cryoprotectants (molecules that are typically used to protect labile ingredients during lyophilization) upon freeze-thaw cycles and lyophilization. The effectiveness of the cyroprotectants evaluated was on the order of trehalose or sucrose > sorbitol > mannitol. The ability of cryoprotectants to prevent GNPs aggregation was dependent on their chemical structure and their ability to interact with the GNPs as assessed with zeta potential analysis.

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“…The non-planar growth of the ice interface was expected because of the high interface speed recorded (Figure 2C), the large thermal gradient imposed (Figure 2B), and the high viscosity of the solution (e.g. supercooled 30 wt% trehalose solution has ten times the viscosity of water at −20°C (Uchida et al, 2009)). Note that the speed of ice growth was faster in lower concentration solutions (Figure 2C).…”

Section: Resultsmentioning

confidence: 99%

Microheterogeneity in frozen protein solutions

Twomey

Kurata

Nagare

et al. 2015

International Journal of Pharmaceutics

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In frozen and lyophilized systems, the biological to be stabilized (e.g. therapeutic protein, biomarker, drug-delivery vesicle) and the cryo-/lyoprotectant should be co-localized for successful stabilization. During freezing and drying, many factors cause physical separation of the biological from the cryo-/lyoprotectant, called microheterogeneity (MH), which may result in poor stabilization efficiency. We have developed a novel technique that utilized confocal Raman microspectroscopy in combination with counter-gradient freezing to evaluate the effect of a wide range of freezing temperatures (−20 < TF < 0°C) on the MH generated within a frozen formulation in only a few experiments. The freezing experiments conducted with a model system (albumin and trehalose) showed the presence of different degrees of MH in the freeze-concentrated liquid (FCL) in all solutions tested. Mainly, albumin tended to accumulate near the ice interface, where it was physically separated from the cryoprotectant. In frozen 10 wt% trehalose solutions, heterogeneity in FCL was relatively low at any TF. In frozen 20 wt% trehalose solutions, the optimum albumin to trehalose ratio in the FCL can only be ensured if the solution was frozen within a narrow range of temperatures (−16 < TF < −10°C). In the 30 wt% trehalose solutions, freezing within a much more narrow range (−12 < TF < −10°C) was needed to ensure a fairly homogeneous FCL. The method developed here will be helpful for the development of uniformly frozen and stable formulations and freezing protocols for biological as MH is presumed to directly impact stability.

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Trehalose solution viscosity at low temperatures measured by dynamic light scattering method: Trehalose depresses molecular transportation for ice crystal growth

Cited by 27 publications

References 30 publications

The Magic of Disaccharide Glass Matrices for Protein Function as Decoded by High-Field EPR and FTIR Spectroscopy

The Magic of Disaccharide Glass Matrices for Protein Function as Decoded by High-Field EPR and FTIR Spectroscopy

Colloidal Stability of Citrate and Mercaptoacetic Acid Capped Gold Nanoparticles upon Lyophilization: Effect of Capping Ligand Attachment and Type of Cryoprotectants

Microheterogeneity in frozen protein solutions

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