The Role of Trehalose for the Stabilization of Proteins

Abstract

Understanding of how the stabilization mechanism of trehalose operates on biological molecules against different types of environmental stress could prove to gain great advancements in many different types of conservation techniques, such as cryopreservation or freeze-drying. Many theories exist that aim to explain why trehalose possesses an extraordinary ability to stabilize biomolecules. However, all of them just explain parts of its mechanism and a comprehensive picture is still lacking. In this study, we have used differential scanning calorimetry (DSC) and viscometry measurements to determine how the glass transition temperature Tg, the protein denaturation temperature Tden, and the dynamic viscosity depend on both the trehalose and the protein concentration in myoglobin-trehalose-water systems. The aim has been to determine whether these physical properties are related and to gain indirect structural insights from the limits of water crystallization at different concentration ratios. The results show that for systems without partial crystallization of water the addition of protein increases Tg, most likely due to the fact that the protein adsorbs water and thereby reduces the water content in the trehalose-water matrix. Furthermore, these systems are generally decreasing in Tden with an increasing protein concentration, and thereby also an increasing viscosity, showing that the dynamics of the trehalose-water matrix and the stability of the native structure of the protein are not necessarily coupled. We also infer, by analyzing the maximum amount of water for which ice formation is avoided, that the preferential hydration model is consistent with our experimental data.

Developmental competence of in vitro matured ovine oocytes vitrified in solutions with different concentrations of trehalose

“…Our experiment also revealed that vitrification in the absence of trehalose (0.0 M) impairs developmental competence in vitri- (Bosch et al, 2016) and stabilizing the structural and functional integrity of cell membrane in lowwater media (Kaushik & Bhat, 2003;Olsson, Jansson, & Swenson, 2016…”

“…Our findings suggest that the detrimental effects of CPAs on ZP were remarkably reduced in the presence of trehalose. Trehalose has been recently found to be useful in preventing the cryodamage (Bosch et al, ) and stabilizing the structural and functional integrity of cell membrane in low‐water media (Kaushik & Bhat, ; Olsson, Jansson, & Swenson, ) . The results of several studies show that stabilizing effects of sugars in general and trehalose in particular, are related to a specific interaction of sugars with biological molecules in bilayer membranes (Jain & Roy, ; Konov et al, ; Olsson et al, ).…”

“…Trehalose has been recently found to be useful in preventing the cryodamage (Bosch et al, ) and stabilizing the structural and functional integrity of cell membrane in low‐water media (Kaushik & Bhat, ; Olsson, Jansson, & Swenson, ) . The results of several studies show that stabilizing effects of sugars in general and trehalose in particular, are related to a specific interaction of sugars with biological molecules in bilayer membranes (Jain & Roy, ; Konov et al, ; Olsson et al, ). Taken together, four major deductions of our study are (a) Trehalose 0.5 M is more efficient, compared to other concentrations, in protecting COCs against damage caused by cooling and warming procedures during vitrification; (b) The incidence of apoptosis in the group vitrified in solution containing 0.5 M trehalose was comparable to that of nonvitrified group suggesting the best developmental potential preservation in this vitrified group; (c) Survival and developmental rates, also blastocyst quality of IVM ovine COCs decreased in the group vitrified in solution containing 1.0 M trehalose suggesting the deleterious effects of high concentrations of trehalose.…”

Crowders and Cosolvents—Major Contributors to the Cellular Milieu and Efficient Means to Counteract Environmental Stresses

“…[137] Althoughb oth thermodynamic models are commonly used to explain and predict the influence of cosolvents on the folding equilibrium of biomolecules, it mayn ot only be the (un)favorable interactions, but also as tructuralo re nergetic change of the hydration shell which favors or disfavors the solvation of hydrophobic and hydrophilic moieties of biomolecules. [138][139][140][141] Furthermore,i tm ust be taken into account that the addition of high concentrations of cosolventc an induce a significant decrease of the water activity and thus generate an osmotics tress that may suck water molecules out from the internal cavities andh ydration shell of the biomolecule. Depending on whether water is released or incorporated upon unfolding, the folding equilibrium will be changed accordingly.…”

Trehalose acts as a uridine 5′‐diphosphoglucose‐competitive inhibitor of trehalose 6‐phosphate synthase in Corynebacterium glutamicum

“…Tre has been recognized as an exceptional protein stabilizer [8,28,29], and this property of Tre is considered crucial to protect cells from stress. A number of studies have been performed to decipher the mechanism of action of Tre [30][31][32].…”