Osmotic Cross Second Virial Coefficient (B23) of Unfavorable Proteins : Modified Lennard-Jones Potential

Sang Ha Choi; Young Chan Bae

Macromolecular Research, Vol.17, No.10, 763-769, October, 2009

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Osmotic Cross Second Virial Coefficient (B23) of Unfavorable Proteins : Modified Lennard-Jones Potential

Sang Ha Choi, and Young Chan Bae^†

Division of Chemical Engineering and Molecular Thermodynamics Lab., Hanyang University, Seoul 133-791, Korea

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A chromatographic method is used to measure interactions between dissimilar proteins in aqueous electrolyte solutions as a function of ionic strength, salt type, and pH. One protein is immobilized on the surface of the stationary phase, and the other is dissolved in electrolyte solution conditions flowing over that surface. The relative retention of proteins reflects the mean interactions between immobile and mobile proteins. The osmotic cross second virial coefficient calculated by assuming a proposed potential function shows that the interactions of unfavorable proteins depend on solution conditions, and the proposed model shows good agreement with the experimental data of the given systems.

Keywords:chromatography;pair potential function;osmotic cross second virial coefficient;MLJ potential

[References]

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Haynes CA, Tamura K, Korfer HR, Blanch HW, Prausnitz JM, J. Phys. Chem., 96, 905 (1992)
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Curtis RA, Prausnitz JM, Blanch HW, Biotechnol. Bioeng., 57(1), 11 (1998)
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Barker JA, Henderson D, J. Chem. Phys., 47, 4714 (1967)
Weeks JD, Chandler D, Andersen HC, J. Chem. Phys., 54, 5237 (1971)
Chang J, Sandler SI, Mol. Phys., 81, 745 (1994)
Teske CA, Blanch HW, Prausnitz JN, J. Phys. Chem. B, 108(22), 7437 (2004)
Domen PL, Nevens JR, Mallia AK, Hermanson GT, Klenk DC, J. Chromatogr., 510, 293 (1990)
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Shen S, Lu BCY, Fluid Phase Equilib., 84, 9 (1993)
Largo J, Solana JR, Phys. A, 284, 68 (2000)
Nicolas JJ, Gubbins KE, Streett WB, Tidesley DJ, Mol. Phys., 37, 1429 (1979)
Kuehner DE, Engmann J, Fergg F, Wernick M, Blanch HW, Prausnitz JM, J. Phys. Chem. B, 103(8), 1368 (1999)
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[Related Articles]

[1] Moon YU, Anderson CO, Blanch HW, Prausnitz JM, Fluid Phase Equilib., 168(2), 229 (2000)

[2] McMillan WG, Mayer JE, J. Chem. Phys., 13, 276 (1945)

[3] Verwey EJW, Overbeek JTG, Theory of the Stability of Lyophobic Colloids, Elsevier, Amsterdam (1948)

[4] Haynes CA, Tamura K, Korfer HR, Blanch HW, Prausnitz JM, J. Phys. Chem., 96, 905 (1992)

[5] Vilker VL, Colton CK, Smith KA, J. Colloid Interface Sci., 79, 548 (1981)

[6] Phillies GD, J. Chem. Phys., 60, 2721 (1974)

[7] Curtis RA, Prausnitz JM, Blanch HW, Biotechnol. Bioeng., 57(1), 11 (1998)

[8] Tessier PM, Lenhoff AM, Sandler SI, Biophis. J., 82, 1620 (2002)

[9] Patro SY, Przybycien TM, Biotechnol. Bioeng., 52(2), 193 (1996)

[10] Tessier PM, Lenhoff AM, Sandler SI, Biophys. J., 82, 1620 (2002)

[11] Tessier PM, Vandrey SD, Berger BW, Pazhianur R, Sandler SI, Lenhoff AM, Acta Crystallogr. Sect. D: Biol. Crystallogr., 58, 1531 (2002)

[12] Tessier PM, Johnson HR, Pazhianur R, Berger BW, Prentice JL, Bahnson BJ, Sandler SI, Lenhoff AM, Proteins: Struct., Funct; Genet., 50, 303 (2003)

[13] Barker JA, Henderson D, J. Chem. Phys., 47, 4714 (1967)

[14] Weeks JD, Chandler D, Andersen HC, J. Chem. Phys., 54, 5237 (1971)

[15] Chang J, Sandler SI, Mol. Phys., 81, 745 (1994)

[16] Teske CA, Blanch HW, Prausnitz JN, J. Phys. Chem. B, 108(22), 7437 (2004)

[17] Domen PL, Nevens JR, Mallia AK, Hermanson GT, Klenk DC, J. Chromatogr., 510, 293 (1990)

[18] Walas SM, Phase Equilibria in Chemical Engineering, Butterworths, Boston, MA (1985)

[19] Shen S, Lu BCY, Fluid Phase Equilib., 84, 9 (1993)

[20] Largo J, Solana JR, Phys. A, 284, 68 (2000)

[21] Nicolas JJ, Gubbins KE, Streett WB, Tidesley DJ, Mol. Phys., 37, 1429 (1979)

[22] Kuehner DE, Engmann J, Fergg F, Wernick M, Blanch HW, Prausnitz JM, J. Phys. Chem. B, 103(8), 1368 (1999)

[23] Kim SG, Bae YC, Macromol. Res., 10, 67 (2003)

[24] Jee NY, Kim JJ, Macromol. Res., 14(6), 654 (2006)