Aggregation of β‐lactoglobulin and influence of D<sub>2</sub>O

Verheul, Marleen; Roefs, S.P.F.M.; Kruif, Kees G. de

doi:10.1016/s0014-5793(97)01581-0

Cited by 36 publications

(39 citation statements)

References 23 publications

(42 reference statements)

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“…Differential scanning calorimetry is particularly useful because the melting temperature, enthalpy, and heat capacity of unfolding can be measured . All but one study reports results similar to ours: D 2 O increases the enthalpy of unfolding . One report shows minimal changes to

normalΔ H_{U}^{°^{'}}

and increases in both T m and

normalΔ G_{U}^{°^{'}}

.…”

Section: Resultssupporting

confidence: 68%

Enthalpic stabilization of an SH3 domain by D₂O

Stadmiller

Pielak

2018

Protein Science

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The stability of a protein is vital for its biological function, and proper folding is partially driven by intermolecular interactions between protein and water. In many studies, H O is replaced by D O because H O interferes with the protein signal. Even this small perturbation, however, affects protein stability. Studies in isotopic waters also might provide insight into the role of solvation and hydrogen bonding in protein folding. Here, we report a complete thermodynamic analysis of the reversible, two-state, thermal unfolding of the metastable, 7-kDa N-terminal src-homology 3 domain of the Drosophila signal transduction protein drk in H O and D O using one-dimensional F NMR spectroscopy. The stabilizing effect of D O compared with H O is enthalpic and has a small to insignificant effect on the temperature of maximum stability, the entropy, and the heat capacity of unfolding. We also provide a concise summary of the literature about the effects of D O on protein stability and integrate our results into this body of data.

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normalΔ H_{U}^{°^{'}}

and increases in both T m and

normalΔ G_{U}^{°^{'}}

.…”

Section: Resultssupporting

confidence: 68%

Enthalpic stabilization of an SH3 domain by D₂O

Stadmiller

Pielak

2018

Protein Science

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“…It is well known that aggregation phenomena for some proteins are influenced by D 2 O. For example, the deuterated solvent stabilized the oligomeric form of halophilic malate dehydrogenase (Bonnete, Madern, & Zaccai, 1994) and is also known to affect the stability of some proteins, such as b-lactoglobulin (Verheul, Roefs, & de Kruif, 1998). Fig.…”

Section: T P In the Presence Of Ca 2+ And Mg 2+ In D 2 Omentioning

confidence: 99%

Temperature dependence of calcium and magnesium induced caseinate precipitation in H2O and D2O

2011

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“…In these studies, many different stabilizers of the physical and chemical states of the antigens were reported and discussed. The protective effects of D 2 O and MgCl 2 on vaccines and proteins were widely demonstrated in different studies . For instance, at relatively high concentrations, D 2 O (>50%) and MgCl 2 (1 M) could reduce the loss of infectivity titers of the poliovirus .…”

Section: Discussionmentioning

confidence: 99%

Role of phenol red in the stabilization of the Sabin type 2 inactivated polio vaccine at various pH values

Yang

Dai

Liu

et al. 2018

Journal of Medical Virology

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To analyze the effects of phenol red at various pH values on the Sabin type 2 inactivated polio vaccine (sIPV2), several biophysical techniques were used to evaluate the particle size and capsid protein for conformation. sIPV2's size was assessed via transmission electron microscopy and dynamic light scattering. The effects of various pH values (from 4.0 to 7.0) on the biophysical characters of sIPV2 particles in solution were determined by dynamic light scattering and zeta potential. The results clearly indicated that aggregation and instability occurred in the solution of sIPV2 particles at a pH of 6.0. Under similar conditions, by dynamic light scattering and zeta potential, the virus particles in solution showed more dispersion and were stable with the addition of 0.05 mM phenol red. According to circular dichroism and intrinsic tryptophan fluorescence data, it was observed that the secondary and tertiary structures of the sIPV2 particles were more stable with the protection of phenol red. At a pH below 6.0, the sIPV2 solution with phenol red had more D-antigen content, which was confirmed by enzyme-linked immunosorbent assay and rat experiments. These results strongly suggested that phenol red improved the pH stability of the sIPV2. The study indicated the potential of phenol red in preserving vaccine potency of the sIPV2 at various pH values.

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Aggregation of β‐lactoglobulin and influence of D₂O

Cited by 36 publications

References 23 publications

Enthalpic stabilization of an SH3 domain by D₂O

Enthalpic stabilization of an SH3 domain by D₂O

Temperature dependence of calcium and magnesium induced caseinate precipitation in H2O and D2O

Role of phenol red in the stabilization of the Sabin type 2 inactivated polio vaccine at various pH values

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Aggregation of β‐lactoglobulin and influence of D2O

Cited by 36 publications

References 23 publications

Enthalpic stabilization of an SH3 domain by D2O

Enthalpic stabilization of an SH3 domain by D2O

Temperature dependence of calcium and magnesium induced caseinate precipitation in H2O and D2O

Role of phenol red in the stabilization of the Sabin type 2 inactivated polio vaccine at various pH values

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Aggregation of β‐lactoglobulin and influence of D₂O

Enthalpic stabilization of an SH3 domain by D₂O

Enthalpic stabilization of an SH3 domain by D₂O