Abstract
Preferential interactions of α-chymotrypsinogen in water and aqueous solutions of ethylene glycol, glycerol, erythritol, sorbitol, and inositol were studied from precise density measurements under conditions of constant molality and constant chemical potential; to achieve the last condition, solutions were brought under equilibrium dialysis. The density measurements were performed at 298.15 K and they were used to determine the preferential interaction parameters. The results confirm a significant correlation between the numbers of hydroxyl groups of the polyols with the stability of α-chymotrypsinogen.
Similar content being viewed by others
Explore related subjects
Discover the latest articles, news and stories from top researchers in related subjects.References
Timasheff, S.N.: Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Adv. Protein Chem. 51, 355–432 (1998)
Timasheff, S.N., Xie, G.: Preferential interactions of urea with lysozyme and their linkage to protein denaturation. Biophys. Chem. 105, 421–448 (2003)
Timasheff, S.N.: In disperse solution, “osmotic stress” is a restricted case of preferential interactions. Proc. Natl. Acad. Sci. USA 95, 7363–7367 (1998)
Arakawa, T., Timasheff, S.N.: The stabilization of proteins by osmolytes. Biophys. J. 47, 411–414 (1985)
Shimizu, S., Smith, D.J.: Preferential hydration and the exclusion of cosolvents from protein surfaces. J. Chem. Phys. 121, 1148–1154 (2004)
McClements, D.J.: Modulation of globular protein functionality by weakly interacting cosolvents. Crit. Rev. Food Sci. Nutr. 42, 417–471 (2002)
Saunders, A.J., Davis-Searles, P.R., Allen, D.L., Pielak, G.J., Erie, D.A.: Osmolyte-induced changes in protein conformational equilibria. Biopolymers 53, 293–307 (2000)
Lee, J.C., Gekko, K., Timasheff, S.N.: Measurements of preferential solvent interactions by densimetric techniques. Methods Enzymol. 61, 26–49 (1979)
Prakash, V.: Partial specific volumes and interactions with solvent components of α-globulin from Sesamum indicum L. in urea and guanidine hydrochloride. J. Biosci. 4, 347–359 (1982)
Schachman, H.K.: Ultracentrifugation, diffusion, and viscometry. Methods Enzymol. 4, 32–103 (1957)
Wayne Kielley, W., Harrington, W.F.: A model for the myosin molecule. Biochim. Biophys. Acta 41, 401–421 (1960)
Casassa, E.F., Eisenberg, H.: Thermodynamic analysis of multicomponent solutions. Adv. Protein Chem. 19, 287–395 (1964)
Cohen, G., Eisenberg, H.: Deoxyribonucleate solutions: sedimentation in a density gradient, partial specific volumes, density and refractive index increments, and preferential interactions. Biopolymers 6, 1077–1100 (1968)
Scatchard, G.: Physical chemistry of protein solutions. I. Derivation of the equations for the osmotic pressure. J. Am. Chem. Soc. 68, 2315–2319 (1946)
Stockmayer, W.H.: Light scattering in multi-component systems. J. Chem. Phys. 18, 58–68 (1950)
Dipaola, G., Belleau, B.: Polyol–water interactions. Apparent molal heat capacities and volumes of aqueous polyol solutions. Can. J. Chem. 55, 3825–3834 (1977)
Romero, C.M., Páez, M.S., Pérez, D.: A comparative study of the volumetric properties of dilute aqueous solutions of 1-propanol, 1,2-propanediol, 1,3-propanediol, and 1,2,3-propanetriol at various temperatures. J. Chem. Thermodyn. 40, 1645–1653 (2008)
Romero, C.M., Lozano, J.M., Giraldo, G.I.: Effect of temperature on partial molar volumes and viscosities of dilute aqueous solutions of 1-butanol, 1,2-butanediol, 1,4-butanediol, 1,2,4-butanetriol, and butanetetrol. J. Chem. Thermodyn. 40, 1645–1653 (2008)
Shanna, S., Larkb, B.S.: Thermodynamic and transport properties of sorbitol and mannitol in water and in mixed aqueous solutions. Indian J. Chem. 38, 6–15 (1999)
Li, H., Xu, X.Y., Chi, C.J., Liu, M., Di, Y.Y., Sun, D.Z.: Molar volumes and refractive indexes of hexane-1,2,3,4,5,6-hexol in aqueous solutions of 1-propanol and 2-propanol. J. Chem. Eng. Data 55, 2909–2913 (2010)
Romero, C.M., Abella, J.S., Velázquez, A., Sancho, J.: Thermal denaturation of α-chymotrypsinogen A in presence of polyols at pH 2.0 and pH 3.0. J. Therm. Anal. Calorim. 120, 489–499 (2015)
Bhat, R., Timasheff, S.N.: Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols. Protein Sci. 1, 1133–1143 (1992)
Gekko, K., Timasheff, S.N.: Mechanism of protein stabilization by glycerol: preferential hydration in glycerol–water mixtures. Biochemistry 20, 4667–4676 (1981)
Xie, G., Timasheff, S.: Mechanism of the stabilization of ribonuclease A by sorbitol: preferential hydration is greater for the denatured than for the native protein. Protein Sci. 6, 211–221 (1997)
Acknowledgements
This work was supported by Universidad Nacional de Colombia, and the National Program of Researches Training 2012 COLCIENCIAS.
Author information
Authors and Affiliations
Contributions
All authors contributed to the study conception and design. Material preparation, data collection and analysis were made by Juan Sebastian Abella and Carmen Maria Romero. The first draft of the manuscript was written by Juan Sebastian Abella and both authors commented on previous versions of the manuscript. All authors read and approved the final manuscript.
Corresponding author
Ethics declarations
Conflict of interest
The authors declare that they have no conflict of interest.
Additional information
Publisher's Note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Rights and permissions
About this article
Cite this article
Abella, J.S., Romero, C.M. Preferential Interaction of Chymotrypsinogen in Aqueous Solutions of Polyols at 298.15 K. J Solution Chem 48, 1591–1602 (2019). https://doi.org/10.1007/s10953-019-00936-5
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s10953-019-00936-5