Modulation of the Hydrogen Bonding Structure of Water by Renal Osmolytes

Verma, Pramod Kumar; Lee, Hochan; Park, Jun Young; Lim, Joon Hyung; Maj, Michał; Choi, Jun Ho; Kwak, Kyung Won; Cho, Minhaeng

doi:10.1021/acs.jpclett.5b01087

Cited by 35 publications

(92 citation statements)

References 39 publications

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“…In contrast, urea shows a weak concentrationdependence of the rotational relaxation dynamics of the OD probe. 29,31,35 Even at very high concentration such as 8 M, the rotational relaxation is similar to that of bulk water, which is again consistent with the notion that urea molecules accommodate well in the tetrahedral network of water without causing significant perturbation to the local water H-bond network.…”

Section: Acs Paragon Plus Environmentsupporting

confidence: 79%

“…31,33 Let us briefly discuss the water- and TMG (green color species). The protecting osmolytes (sorbitol and TMG) adopt to a network-like aggregate structure in their highly concentrated aqueous solutions that is morphologically similar to that of the extended water H-bond network.…”

Section: B Osmolyte Aggregate and Water H-bonding Network Structuresmentioning

confidence: 99%

“…73 Our recent experimental data have revealed that the vibrational population lifetime of the OD stretch band is marginally dependent on the type and concentration of osmolytes. 31 Moreover, 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 16 because the vibrational lifetime broadening is negligible in comparison to the effects from the distributions of the O-D frequencies as well as the O-D stretch transition dipole moments due to heterogeneous electrostatic environment. The IR absorption spectrum of the OD stretch mode depends mostly on the contributions from the inhomogeneous broadening as well as varying transition dipole moment due to non-Condon effect, rather than the vibrational lifetime.…”

Section: A Numerically Simulated O-d Ir Absorption Spectra In Aqueoumentioning

confidence: 99%

“…In general, addition of osmolytes retards the rotational relaxation, but the extent of retardation depends on the type of the osmolyte. 29,31,32 In pure water, complete reorientation relaxation involves both breaking and reforming of H-bonds via water molecules in a special H-bonded configuration in which the hydroxyl group forms a weak, bifurcated H-bond to two other water molecules. Any process that limits the accessibility of the new H-bond acceptor during the H-bond exchange process will slow down the rotational relaxation.…”

Section: Acs Paragon Plus Environmentmentioning

confidence: 99%

“…18 Therefore, it has been routinely used to investigate the water H-bonding dynamics in not just bulk water, 13,14,[19][20][21][22] but also other solutions containing salts, [23][24][25][26] watermiscible organic solvent molecules, 27,28 and osmolytes. [29][30][31][32] More precisely, the HDO has the capability to form multiple H-bonds with surrounding water molecules as well as other dissolved species (osmolyte, amphiphile, salt, etc.). Consequently, its vibrational dynamics provides important information from HDO's point of view on H-bond making and breaking processes and solvation dynamics.…”

Section: Introductionmentioning

confidence: 99%

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Computational Vibrational Spectroscopy of HDO in Osmolyte–Water Solutions

et al. 2016

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The IR absorption and time-resolved IR spectroscopy of the OD stretch mode of HDO in water was successfully used to study osmolyte effects on water H-bonding network. Protecting osmolytes such as sorbitol and trimethylglycine (TMG) make the vibrational OD stretch band red-shifted, whereas urea affects the OD band marginally. Furthermore, we recently showed that, even though sorbitol and TMG cause a slow-down of HDO rotation in their aqueous solutions, urea does not induce any change in the rotational relaxation of HDO in aqueous urea solutions even at high concentrations. To clarify the underlying osmolyte effects on water H-bonding structure and dynamics, we performed molecular dynamics (MD) simulations of a variety of aqueous osmolyte solutions. Using the vibrational solvatochromism model for the OD stretch mode and taking into account the vibrational non-Condon and polarization effects on the OD transition dipole moment, we then calculated the IR absorption spectra and rotational anisotropy decay of the OD stretch mode of HDO for the sake of direct comparisons with our experimental results. The simulation results on the OD stretch IR absorption spectra and the rotational relaxation rate of HDO in osmolyte solutions are found to be in quantitative agreement with experimental data, which confirms the validity of the MD simulation and vibrational solvatochromism approaches. As a result, it becomes clear that the protecting osmolytes like sorbitol and TMG significantly modulate water H-bonding network structure, while urea perturbs water structure little. We anticipate that the computational approach discussed here will serve as an interpretive method with atomic-level chemical accuracy of current linear and nonlinear time-resolved IR spectroscopy of structure and dynamics of water near the surfaces of membranes and proteins under crowded environments.

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Section: Acs Paragon Plus Environmentsupporting

confidence: 79%

Section: B Osmolyte Aggregate and Water H-bonding Network Structuresmentioning

confidence: 99%

Section: A Numerically Simulated O-d Ir Absorption Spectra In Aqueoumentioning

confidence: 99%

Section: Acs Paragon Plus Environmentmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Computational Vibrational Spectroscopy of HDO in Osmolyte–Water Solutions

et al. 2016

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A generalized purification step for viral particles using mannitol flocculation

Heldt

Saksule

Joshi

et al. 2018

Biotechnology Progress

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Vaccine manufacturing has conventionally been performed by the developed world using traditional unit operations like filtration and chromatography. There is currently a shift in the manufacturing of vaccines to the less developed world, requiring unit operations that reduce costs, increase recovery, and are amenable to continuous manufacturing. This work demonstrates that mannitol can be used as a flocculant for an enveloped and nonenveloped virus and can purify the virus from protein contaminants after microfiltration. The recovery of the virus ranges from 58 to 96% depending on virus, the filter pore size, and the starting concentration of the virus. Protein removal of 80% was achieved for the small nonenveloped virus using a 0.1 µm filter because proteins were not flocculated with the virus and flowed through the filter. It is hypothesized that mannitol dehydrates the viral surface by controlling the water structure surrounding the virus. Without the ability to become compact, as occurs with proteins, the virus aggregates in the presence of osmolytes and proteins do not. Osmolyte flocculation is a scalable process using high flux microfilters. It has been applied to both an enveloped and nonenveloped virus, making this process friendly to a variety of vaccine and gene therapy products. © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 34:1027-1035, 2018.

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

et al. 2017

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The free energy and conformational landscape of biomolecular systems as well as biochemical reactions depend not only on temperature and pressure, but also on the particular solution conditions. Such conditions include the effects of cosolvents (for example osmolytes) and macromolecular crowding, which are crucial components to understand the energetics and kinetics of biological processes in living system. Such conditions are also important for the understanding of many debilitating diseases, such as those where misfolding and amyloid formation of proteins are involved. Moreover, understanding their effects on biomolecular processes is prerequisite for designing industrially relevant enzymatic reactions, which seldom take place under neat conditions. Here, we review and discuss experimental and theoretical studies on the characterization of cosolvent and crowding induced effects in biologically relevant systems, approaching even the complexity of living organisms. In particular, we focus on cosolvent and crowding effects on the conformational equilibrium and folding kinetics of proteins and nucleic acids as well as on enzymatic reactions, including their effects on the temperature and pressure dependence of these processes. By presenting a few representative examples, we show how such effects are unveiled and described in thermodynamic and kinetic terms.

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Modulation of the Hydrogen Bonding Structure of Water by Renal Osmolytes

Cited by 35 publications

References 39 publications

Computational Vibrational Spectroscopy of HDO in Osmolyte–Water Solutions

Computational Vibrational Spectroscopy of HDO in Osmolyte–Water Solutions

A generalized purification step for viral particles using mannitol flocculation

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

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