Solubility and prenucleation of aprotinin (BPTI) molecules in sodium chloride solutions

Lafont, Sylvaine; Veesler, Stéphane; Astier, Jean-Pierre; Boistelle, R.

doi:10.1016/0022-0248(94)90064-7

Cited by 40 publications

(49 citation statements)

References 16 publications

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“…about 1.5 times higher at basic than at acidic pH (about 70.4% versus 48.5% for 6 mg/ml and about 79.0% versus 53.1% for 9 mg/ml). Since monodispersity is established for Ͻ 6% (27), it clearly indicates that lithostathine solutions are polydispersed. However, at acidic pH the values of the hydrodynamic radius ϽR H Ͼ at 6 and 9 mg/ml are about 1.3 nm whereas at basic pH, both values turn around 38 nm.…”

Section: Resultsmentioning

confidence: 99%

“…This reflects the high degree of homogeneity of the lithostathine preparation. The hydrodynamic non-ideality of lithostathine causes a negative dependence of the sedimentation coefficient s 20 pH and CaCl 2 Effects on Diffusion Coefficient and Polydispersity of Lithostathine-QELS experiments have been undertaken because of their advantage of rapid analysis, without perturbation of the system, thereby facilitating the study of macromolecules in solution (27)(28)(29)(30)(31)(32)(33)(34). Table I summarized the main parameters measured by these experiments.…”

Section: Resultsmentioning

confidence: 99%

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Biophysical Characterization of Lithostathine

Cérini

Peyrot

Garnier

et al. 1999

Journal of Biological Chemistry

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Lithostathine is a calcium carbonate crystal habit modifier. It is found precipitated under the form of fibrils in chronic calcifying pancreatitis or Alzheimer's disease. In order to gain better insight into the nature and the formation of fibrils, we have expressed and purified recombinant lithostathine. Analytical ultracentrifugation and quasi-elastic light scattering techniques were used to demonstrate that lithostathine remains essentially monomeric at acidic pH while it aggregates at physiological pH. Analysis of these aggregates by electron microscopy showed an apparently unorganized structure of numerous monomers which tend to precipitate forming regular unbranched fibrils. Aggregated forms seem to occur prior to the apparition of fibrils. In addition, we have demonstrated that these fibrils resulted from a proteolysis mechanism due to a specific cleavage of the Arg 11 -Ile 12 peptide bond. It is deduced that the NH 2 -terminal undecapeptide of lithostathine normally impedes fiber formation but not aggregation. A theoretical model explaining the formation of amyloid plaques in neurodegenerative diseases or stones in lithiasis starting from lithostathine is described. Therefore we propose that lithostathine, whose major function is unknown, defines a new class of molecules which is activated by proteolysis and is not involved in cytoskeleton nor intermediate filament functions.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Biophysical Characterization of Lithostathine

Cérini

Peyrot

Garnier

et al. 1999

Journal of Biological Chemistry

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“…For the second batch, see the next section. 18 and the TL-L boundary curve from Grouazel et al 37 (b) The complete TL-L boundary curve (this study); error bars for C < 200 mg/mL have the size of the point on the graph and solid line is a guideline. The circle is a point of the solidus line.…”

Section: Scattering Studies Of Bpti Supersaturated Solutionsmentioning

confidence: 99%

“…3 Protein phase separations can also be the cause of human diseases, such as cataract 4 or sickle cell disease. 5 Despite their fundamental importance, phase diagrams of only a few proteins have been studied: insulin, 6 fibrinogen, 7 γ-crystallin, 8 lysozyme, 4,9-12 concanavalin, 13 canavalin, 14 R-amylase, 15,16 collagenase, 17 bovine pancreatic trypsin inhibitor (BPTI), 16,18 apoferritin, 19 endoglucanase A, 20 and the photochemical reaction center from Rhodobacter sphaeroides Y. 21 Recently, there has been a renewed enthusiasm for phasetransition studies of colloids 22 and proteins [22][23][24][25][26][27] due to advances in experimental and computational technologies.…”

Section: Introductionmentioning

confidence: 99%

Exploring Bovine Pancreatic Trypsin Inhibitor Phase Transitions

et al. 2006

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This paper presents an investigation of the phase diagram of BPTI (bovine pancreatic trypsin inhibitor)/350 mM KSCN at pH 4.9 by direct observation and numerical simulations. We report optical microscopy and light and X-ray scattering experiments coupled with theoretical data analysis using numerical tools. The phase diagram is thoroughly determined, as a function of temperature. Two polymorphs are observed by video microscopy and their solubility measured. In this phase diagram, the liquid-liquid phase separation (LLPS) is metastable with respect to the solid-liquid phase separation. Above the T L-L boundary curve, solutions are composed of a mixture of BPTI monomers and decamers. Attractive interactions are stronger between decamers than between monomers. Below the T L-L boundary curve, the dense phase is highly concentrated in protein and composed of BPTI decamers alone. Thus, the driving force for liquid-liquid or liquid-solid phase separation is the attraction between decamers at low pH. The structure factors of the dense phases are characteristic of repulsive dense phases because of a hard sphere repulsion core, meaning that in the dense phase proteins are actually in contact (interparticle distance of 53 Å). In agreement with the Oswald rule of stages, LLPS occurs prior to and impedes the solid nucleation.

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“…These may, in turn, be applied under different physical conditions such as temperature, which can be an important variable in biological macromolecule crystallization, since an understanding of the phase diagram is useful for the production of suitable crystals for structural biology (Boistelle et al 1992;Lafont et al 1994Lafont et al , 1997Revalor et al 2010). …”

Section: Effect Of Temperature On the Solubilitymentioning

confidence: 99%

Crystallization, solubility and thermodynamics of the highly thermostable glucose isomerase from Streptomyces sp. strain

Borgi¹,

Rhimi²,

Kadri³

2014

gpb

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Abstract. The crystallization behaviour of the highly thermostable glucose isomerase from the Streptomyces sp. strain isolated from Tunisian soil was investigated using ammonium sulfate as a precipitating agent. We established phase diagrams at different temperatures and protein concentrations. It was found that the solubility increased with increasing temperature and decreased with increasing salt concentration. The temperature-dependent solubility was used to characterize the thermodynamic parameters of crystallization such as enthalpy, entropy and free energy.

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Solubility and prenucleation of aprotinin (BPTI) molecules in sodium chloride solutions

Cited by 40 publications

References 16 publications

Biophysical Characterization of Lithostathine

Biophysical Characterization of Lithostathine

Exploring Bovine Pancreatic Trypsin Inhibitor Phase Transitions

Crystallization, solubility and thermodynamics of the highly thermostable glucose isomerase from Streptomyces sp. strain

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