Determination of the second virial coefficient of bovine serum albumin under varying pH and ionic strength by composition-gradient multi-angle static light scattering

Journal of Biological Physics

Volumn 41, Issue 1, 2015, Pages 85-97

  Ma, Yingfang ^a   Acosta, Diana M ^b   Whitney, Jon R ^b   Podgornik, Rudolf ^c,d,e   Steinmetz, Nicole F ^a,f   French, Roger H ^a,g   Parsegian, V Adrian ^c  

^a Case Western Reserve University   (United States)

^b Case Western Reserve University   (United States)

^c UNIVERSITY OF MASSACHUSETTS   (United States)

^d JO EF STEFAN INSTITUTE   (Slovenia)

^e UNIVERSITY OF LJUBLJANA   (Slovenia)

^f CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^g CASE WESTERN RESERVE UNIVERSITY   (United States)

Author keywords

BSA; Electrostatic interactions; Long range interactions; Second virial coefficient; van der Waals interactions

Indexed keywords

BOVINE SERUM ALBUMIN; SODIUM CHLORIDE; PROTEIN BINDING;

AQUEOUS SOLUTION; ARTICLE; COMPOSITION GRADIENT MULTI ANGLE STATIC LIGHT SCATTERING; CONTROLLED STUDY; ILLUMINATION; IONIC STRENGTH; ISOELECTRIC POINT; LIGHT SCATTERING; MATHEMATICAL PARAMETERS; MEASUREMENT ACCURACY; MOLECULAR INTERACTION; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; SECOND VIRIAL COEFFICIENT; STATIC ELECTRICITY; ANIMAL; BOVINE; CHEMISTRY; DRUG EFFECTS; HYDRODYNAMICS; LIGHT; METABOLISM; OSMOLARITY; RADIATION SCATTERING;

ANIMALS; CATTLE; HYDRODYNAMICS; LIGHT; OSMOLAR CONCENTRATION; PROTEIN BINDING; SCATTERING, RADIATION; SERUM ALBUMIN, BOVINE; SODIUM CHLORIDE; STATIC ELECTRICITY;

EID: 84922104982     PISSN: 00920606     EISSN: 15730689     Source Type: Journal    
DOI: 10.1007/s10867-014-9367-7     Document Type: Article

References (62)

1. French, R.H., Parsegian, V.A., Podgornik, R., Rajter, R.F., Jagota, A., Luo, J., Asthagiri, D., Chaudhury, M.K., Chiang, Y.-m., Granick, S., Kalinin, S., Kardar, M., Kjellander, R., Langreth, D.C., Lewis, J., Lustig, S., Wesolowski, D., Wettlaufer, J.S., Ching, W.-Y., Finnis, M., Houlihan, F., von Lilienfeld, O.A., van Oss, C.J., Zemb, T.: Long range interactions in nanoscale sciences. Rev. Mod. Phys. 82, 1887–1944 (2010)
2. Leckband, D., Israelachvili, J.: Intermolecular forces in biology. Q. Rev. Biophys. 34(02), 105–267 (2001)
3. Nel, A.E., Mdler, L., Velegol, D., Xia, T., Hoek, E.M.V., Somasundaran, P., Klaessig, F., Castranova, V., Thompson, M.: Understanding biophysicochemical interactions at the nanobio interface. Nat. Mater. 8, 543–557 (2009)
4. Piazza, R.: Protein interactions and association: an open challenge for colloid science. Curr. Opin. Colloid Interface Sci. 8, 515–522 (2004)
5. Leckband, D., Sivasankar, S.: Forces controlling protein interactions: theory and experiment. Colloids Surf. B: Biointerfaces 14, 83–97 (1999)
6. Jones, S., Thornton, J.M.: Principles of protein-protein interactions. Proc. Natl. Acad. Sci. U.S.A 93, 13–20 (1996)
7. Rao, V.S., Srinivas, K., Sujini, G.N., Kumar, G.N.S.: Protein-protein interaction detection: Methods and analysis. Intl. J. Proteomics 2014, 147648 (2014)
8. Frokjaer, S., Otzen, D.E.: Protein drug stability: a formulation challenge. Nat. Rev. Drug Discov. 4, 298–306 (2005)
9. George, A., Wilson, W.W.: Predicting protein crystallization from a dilute solution property. Acta Crystallogr. D Biol. Crystallogr. 50, 361–365 (1994)
10. Ramirez-Alvarado, M., Merkel, J.S., Regan, L.: A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc. Natl. Acad. Sci. U. S. A. 97, 8979–8984 (2000)
11. Verwey, E.J.W.: Theory of the stability of lyophobic colloids the interaction of sol particles having an electric double layer. Elsevier, New York (1948)
12. van Oss, C.J: Interfacial Forces in Aqueous Media. CRC Press (994)
13. Parsegian, V.A.: Van der Waals forces: a handbook for biologists, chemists, engineers, and physicists. Cambridge University Press (2006)
14. Bozic, A.L., Podgornik, R.: Symmetry effects in electrostatic interactions between two arbitrarily charged spherical shells in the debye-hückel approximation. J. Chem. Phys. 138(7), 074902 (2013). arXiv: http://arxiv.org/abs/1211.5324[cond-mat]
15. Liang, Y., Hilal, N., Langston, P., Starov, V.: Interaction forces between colloidal particles in liquid: Theory and experiment. Adv. Colloid Interf. Sci. 134–135, 151–166 (2007)
16. Neal, B.L., Asthagiri, D., Lenhoff, A.M.: Molecular origins of osmotic second virial coefficients of proteins. Biophys. J. 75, 2469–2477 (1998)
17. Salis, A., Bostrom, M., Medda, L., Cugia, F., Barse, B., Parsons, D. F., Ninham, B. W., Monduzzi, M.: Measurements and theoretical interpretation of points of zero charge/potential of BSA protein. Langmuir 27, 11597–11604 (2011)
18. Roth, C.M., Neal, B.L., Lenhoff, A.M.: Van der Waals interactions involving proteins. Biophys. J. 70, 977–987 (1996)
19. Arzenek, D., Kuzman, D., Podgornik, R.: Colloidal interactions between monoclonal antibodies in aqueous solutions. J. Colloid Interface Sci. 384, 207–216 (2012)
20. Wu, J., Prausnitz, J.M.: Osmotic pressures of aqueous bovine serum albumin solutions at high ionic strength. Fluid Phase Equilib. 155, 139–154 (1999)
21. Hill, T.L.: An Introduction to Statistical Thermodynamics. Courier Dover Publications (2012)
22. Sahin, E., Grillo, A.O., Perkins, M.D., Roberts, C.J.: Comparative effects of pH and ionic strength on proteinprotein interactions, unfolding, and aggregation for IgG1 antibodies. J. Pharm. Sci. 99, 4830–4848 (2010)
23. Blanco, M.A., Sahin, E., Li, Y., Roberts, C.J.J.: Reexamining proteinprotein and proteinsolvent interactions from kirkwood-buff analysis of light scattering in multi-component solutions. J. Chem. Phys. 134, 225103 (2011)
24. Vilker, V.L., Colton, C.K., Smith, K.A.: The osmotic pressure of concentrated protein solutions: Effect of concentration and ph in saline solutions of bovine serum albumin. J. Colloid Interface Sci. 79, 548–566 (1981)
25. Haynes, C.A., Tamura, K., Korfer, H.R., Blanch, H.W., Prausnitz, J.M.: Thermodynamic properties of aqueous α-chymotrypsin solution from membrane osmometry measurements. J. Phys. Chem. 96, 905–912 (1992)
26. Moon, Y.U., Curtis, R.A., Anderson, C.O., Blanch, H.W., Prausnitz, J.M.: Proteinprotein interactions in aqueous ammonium sulfate solutions. lysozyme and bovine serum albumin (BSA). J. Solut. Chem. 29, 699–718 (2000)
27. 4 solution at 25 c by osmotic pressure measurements. J. Chem. Eng. Data 54, 1975–1980 (2009)
28. Park, Y., Choi, G.: Effects of pH, salt type, and ionic strength on the second virial coefficients of aqueous bovine serum albumin solutions. Korean J. Chem. Eng. 26(1), 193–198 (2009)
29. Bonnet, F., Finet, S., Tardieu, A.: Second virial coefficient: variations with lysozyme crystallization conditions. J. Cryst. Growth 196, 403–414 (1999)
30. Bonnet, F., Vivars, D.: Interest of the normalized second virial coefficient and interaction potentials for crystallizing large macromolecules. Acta Crystallogr. D Biol. Crystallogr. 58, 1571–1575 (2002)
31. Tardieu, A., Le Verge, A., Malfois, M., Bonnet, F., Finet, S., Ris-Kautt, M., Belloni, L.: Proteins in solution: from x-ray scattering intensities to interaction potentials. J. Cryst. Growth 196, 193–203 (1999)
32. 2O. J. Cryst. Growth 178, 575–584 (1997)
33. Velev, O.D., Kaler, E.W., Lenhoff, A.M.: Protein interactions in solution characterized by light and neutron scattering: Comparison of lysozyme and chymotrypsinogen. Biophys. J. 75, 2682–2697 (1998)
34. Behlke, J., Ristau, O.: Analysis of the thermodynamic non-ideality of proteins by sedimentation equilibrium experiments. Biophys. Chem. 76, 13–23 (1999)
35. Winzor, D.J., Deszczynski, M., Harding, S.E., Wills, P.R.: Nonequivalence of second virial coefficients from sedimentation equilibrium and static light scattering studies of protein solutions. Biophys. Chem. 128, 46–55 (2007)
36. Tessier, P.M., Lenhoff, A.M., Sandler, S.I.: Rapid measurement of protein osmotic second virial coefficients by self-interaction chromatography. Biophys. J. 82, 1620–1631 (2002)
37. Dumetz, A., O’Brien, A., Kaler, E., Lenhoff, A.: Patterns of protein-protein interactions in salt solutions and implications for protein crystallization. Protein Sci. 16(9), 1867–1877 (2007)
38. Shearwin, K.E., Winzor, D.J.: Thermodynamic nonideality in macromolecular solutions. Eur. J. Biochem. 190, 523–529 (1990)
39. Bajaj, H., Sharma, V.K., Kalonia, D.S.: Determination of second virial coefficient of proteins using a dual-detector cell for simultaneous measurement of scattered light intensity and concentration in SEC-HPLC. Biophys. J. 87, 4048–4055 (2004)
40. Bloustine, J., Berejnov, V., Fraden, S.: Measurements of protein-protein interactions by size exclusion chromatography. Biophys. J. 85, 2619–2623 (2003)
41. Agena, S.M., Bogle, I.D.L., Pessoa, F.L.P.: An activity coefficient model for proteins. Biotechnol. Bioeng. 55, 65–71 (1997)
42. Guo, B., Kao, S., McDonald, H., Asanov, A., Combs, L.L., William Wilson, W.: Correlation of second virial coefficients and solubilities useful in protein crystal growth. J. Cryst. Growth 196, 424–433 (1999)
43. Fernández, C., Minton, A.P.: Static light scattering from concentrated protein solutions II: Experimental test of theory for protein mixtures and weakly self-associating proteins. Biophys. J. 96, 1992–1998 (2009)
44. Fernández, C., Minton, A.P.: Effect of nonadditive repulsive intermolecular interactions on the light scattering of concentrated proteinosmolyte mixtures. J. Phys. Chem. B 115, 1289–1293 (2011)
45. Bajaj, H., Sharma, V.K., Kalonia, D.S.: A high-throughput method for detection of protein self-association and second virial coefficient using size-exclusion chromatography through simultaneous measurement of concentration and scattered light intensity. Pharm. Res. 24, 2071–2083 (2007)
46. Some, D., Hitchner, E., Ferullo, J.: Characterizing protein-protein interactions via static light scattering: Nonspecific interactions. American Biotechnology Laboratory 27(2), 16 (2009)
47. Some, D.: Light-scattering-based analysis of biomolecular interactions. Biophys. Rev. 5, 147–158 (2013)
48. Attri, A.K., Minton, A.P.: New methods for measuring macromolecular interactions in solution via static light scattering: basic methodology and application to nonassociating and self-associating proteins. Anal. Biochem. 337, 103–110 (2005)
49. Zimm, B.H.: The scattering of light and the radial distribution function of high polymer solutions. J. Chem. Phys. 16, 1093–1099 (1948)
50. Roberts, D., Keeling, R., Tracka, M., van der Walle, C.F., Uddin, S., Warwicker, J., Curtis, R.: The role of electrostatics in proteinprotein interactions of a monoclonal antibody. Mol. Pharmaceutics 11, 2475–2489 (2014)
51. Tanford, C., Buzzell, J.G.: The viscosity of aqueous solutions of bovine serum albumin between pH 4.3 and 10.5. J. Phys. Chem. 60, 225–231 (1956)
52. Jachimska, B., Wasilewska, M., Adamczyk, Z.: Characterization of globular protein solutions by dynamic light scattering, electrophoretic mobility, and viscosity measurements. Langmuir 24, 6866–6872 (2008)
53. Jachimska, B., Pajor, A.: Physico-chemical characterization of bovine serum albumin in solution and as deposited on surfaces. Bioelectrochem. 87, 138–146 (2012)
54. Squire, P. G., Moser, P., O’Konski, C. T.: Hydrodynamic properties of bovine serum albumin monomer and dimer. Biochem. 7, 4261–4272 (1968)
55. Liu, F., Liu, T., Qu, M., Yang, Q.: Molecular and biochemical characterization of a novel β-N-Acetyl-D-hexosaminidase with broad substrate-spectrum from the aisan corn borer, Ostrinia Furnacalis. Int. J. Biol. Sci. 8(8), 1085–1096 (2012)
56. Schumaker, V.N.: Lipoproteins, Apolipoproteins, and Lipases. Academic Press (1994)
57. Salgın, S., Salgın, U., Bahadır, S: Zeta potentials and isoelectric points of biomolecules: The effects of ion types and ionic strengths. Int. J. Electrochem. Sci. 7, 12404–12414 (2012)
58. Ra, A.: A study of the variation of the average isoelectric points of several plasma proteins with ionic strength. J. Phys Colloid Chem. 53, 114–126 (1949)
59. Parsegian, V.A., Ninham, B.W.: Temperature-dependent van der Waals forces. Biophys. J. 10, 664–674 (1970)
60. Ninham, B.W., Parsegian, V.A.: van der Waals forces: Special characteristics in lipid-water systems and a general method of calculation based on the Lifshitz theory. Biophys. J. 10, 646–663 (1970)
61. Steinmetz, N.F., Manchester, M.: Viral Nanoparticles: Tools for Material Science and Biomedicine, 1st ed. Pan Stanford Publishing, Singapore (2011)
62. Hemminger, J.: From Quanta to the Continuum: Opportunities for Mesoscale Science. U.S Department of Energy Basic Energy Sciences Advisory Committee (2012)