Modes of interaction of cryoprotectants with membrane phospholipids during freezing

Anchordoguy, Thomas J.; Rudolph, Alan S.; Carpenter, John F.; Crowe, John H.

doi:10.1016/0011-2240(87)90036-8

Cited by 399 publications

(158 citation statements)

References 29 publications

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“…94,248 The effects of various lyoprotectants, including trehalose, on the structural integrity of liposomes have been examined. Some of the main observations include the lowering of T m , 34,243,249 inhibition of aggregation/fusion 249,250 and inhibition of phase separation, 94,248 all of which contribute to the enhanced stability of liposomes. T m indicates the temperature at which the membrane lipids undergo a transition from the gel phase (T < T m ) to the liquid crystalline phase (T > T m ).…”

Section: Proteins and Enzymesmentioning

confidence: 99%

Trehalose: Current Use and Future Applications

Ohtake

Wang²

2011

Journal of Pharmaceutical Sciences

396

261

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Section: Proteins and Enzymesmentioning

confidence: 99%

Trehalose: Current Use and Future Applications

Ohtake

Wang²

2011

Journal of Pharmaceutical Sciences

396

261

View full text Add to dashboard Cite

“…Such interactions are not fully understood, despite numerous studies comparing their empirical effectiveness in cellular cryopreservation. [3][4][5][6][7] By utilizing concurrent surface water diffusivity and equilibrium surface forces measurements, the present work suggests that the two molecules influence membrane hydration differently, with DMSO effectively desolvating the surface and glycerol strengthening surface hydration, but only as much as glycerol increases the bulk water viscosity. Similar comparisons on surface hydration between DMSO and glycerol have been raised in studies on model peptides, largely through neutron scattering measurements, 8,9 but direct comparisons of the effects of these cryoprotectants on lipid membrane systems remain absent.…”

Section: Introductionmentioning

confidence: 99%

Communication: Contrasting effects of glycerol and DMSO on lipid membrane surface hydration dynamics and forces

Schrader

Cheng

Israelachvili

et al. 2016

The Journal of Chemical Physics

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Water structure around hydrophobic amino acid side chain analogs using different water models The Journal of Chemical Physics 146, 225104 (2017) Glycerol and dimethyl sulfoxide (DMSO) are commonly used cryoprotectants in cellular systems, but due to the challenges of measuring the properties of surface-bound solvent, fundamental questions remain regarding the concentration, interactions, and conformation of these solutes at lipid membrane surfaces. We measured the surface water diffusivity at gel-phase dipalmitoylphosphatidylcholine (DPPC) bilayer surfaces in aqueous solutions containing ≤7.5 mol. % of DMSO or glycerol using Overhauser dynamic nuclear polarization. We found that glycerol similarly affects the diffusivity of water near the bilayer surface and that in the bulk solution (within 20%), while DMSO substantially increases the diffusivity of surface water relative to bulk water. We compare these measurements of water dynamics with those of equilibrium forces between DPPC bilayers in the same solvent mixtures. DMSO greatly decreases the range and magnitude of the repulsive forces between the bilayers, whereas glycerol increases it. We propose that the differences in hydrogen bonding capability of the two solutes leads DMSO to dehydrate the lipid head groups, while glycerol affects surface hydration only as much as it affects the bulk water properties. The results suggest that the mechanism of the two most common cryoprotectants must be fundamentally different: in the case of DMSO by decoupling the solvent from the lipid surface, and in the case of glycerol by altering the hydrogen bond structure and intermolecular cohesion of the global solvent, as manifested by increased solvent viscosity. Published by AIP Publishing.[http://dx

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“…These molecules lend protection to proteins against such denaturing stresses, without interfering with their functionality. It is believed that this compatibility results from the absence of interactions between osmolytes and substrates or cofactors [5].…”

Section: Introductionmentioning

confidence: 99%

“…The cryoprotective properties of this family of compounds were also the aim of several studies In fact, it was demonstrated that sarcosine, in concentrations greater than 1 M, reduces fusion and leakage of liposomes after freeze-thaw, by interacting with the acyl chains of the lipid bilayer [5][6][7][8].…”

Section: Introductionmentioning

confidence: 99%

Conformational study of sarcosine as probed by matrix-isolation FT-IR spectroscopy and molecular orbital calculations

Gómez‐Zavaglia

Fausto

2003

Vibrational Spectroscopy

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Sarcosine (N-methylglycine) has been studied by matrix-isolation FT-IR spectroscopy and molecular orbital calculations undertaken at the DFT/B3LYP and MP2 levels of theory with the 6-311þþG(d, p) and 6-31þþG(d, p) basis set, respectively. Eleven different conformers were located in the potential energy surface (PES) of sarcosine, with the ASC conformer being the ground conformational state. This form is analogous to the glycine most stable conformer and is characterized by a NH Á Á Á O= intramolecular hydrogen bond; in this form, the carboxylic group assumes the cis configuration and the O=C-C-N and Lp-N-C-C (where Lp is the nitrogen lone electron pair) dihedral angles are ca. 15 and À88, respectively. The second most stable conformer (G 0 AT) exhibits a strong OH Á Á Á N intramolecular hydrogen bond and a trans carboxylic group, being similar to the most stable form of N,N-dimethylglycine. These two forms were predicted to differ in energy by less than ca. 2 kJ mol À1 and represent %70% of the conformational population at room temperature. In consonance with the theoretical predictions, the FT-IR spectra of the matrix-isolated compound reveal the presence in the gaseous phase of the four conformers of sarcosine with experimentally accessible populations: besides conformers ASC and G 0 AT, forms GSC and AAC could also be identified experimentally. The assignment of the spectra of the different experimentally observed conformers of sarcosine was carried out. #

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Modes of interaction of cryoprotectants with membrane phospholipids during freezing

Cited by 399 publications

References 29 publications

Trehalose: Current Use and Future Applications

Trehalose: Current Use and Future Applications

Communication: Contrasting effects of glycerol and DMSO on lipid membrane surface hydration dynamics and forces

Conformational study of sarcosine as probed by matrix-isolation FT-IR spectroscopy and molecular orbital calculations

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