Self-interaction chromatography: A tool for the study of protein- protein interactions in bioprocessing environments

Biotechnology and Bioengineering

Volumn 52, Issue 2, 1996, Pages 193-203

  Patro, Sugunakar Y ^a   Przybycien, Todd M ^a  

^a Rensselaer Polytechnic Institute   (United States)

Author keywords

affinity chromatography; excipient screening; protein aggregation; protein formulation; specific interaction sites

Indexed keywords

ADDITIVES; AGGLOMERATION; BINDING ENERGY; CRYSTAL STRUCTURE; ISOTHERMS; MATHEMATICAL MODELS; MOLECULAR DYNAMICS; PROTEINS; STABILIZERS (AGENTS);

BINDING ISOTHERM MODEL; EXCIPIENT SCREENING; PROTEIN AGGREGATION; PROTEIN FORMULATION; PROTEIN PROTEIN INTERACTIONS; SELF INTERACTION CHROMATOGRAPHY; SPECIFIC INTERACTION SITES;

AFFINITY CHROMATOGRAPHY;

DEXTRAN 40; GLYCINE; MANNITOL;

BINDING AFFINITY; CHROMATOGRAPHY; CONFERENCE PAPER; ENZYME BINDING; ENZYME STABILITY; MOLECULAR INTERACTION; PROTEIN AGGREGATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION;

EID: 10144225635     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19961020)52:2<193::AID-BIT2>3.0.CO;2-L     Document Type: Conference Paper

References (60)

1. Anonymous. 1993. Affinity chromatography: Principles and methods. Pharmacia LKB Biotechnology, Sweden.
2. Arakawa, T. 1989. The stabilization of β-lactoglobulin by glycine and NaCl. Biopolymers 28: 1397-1401.
3. Arakawa, T., Timasheff, S. N. 1982. Stabilization of protein structure by sugars. Biochemistry 21: 6536.
4. Arakawa, T., Timasheff, S. N. 1983. Preferential interactions of proteins with solvent components in aqueous amino acid solutions. Arch. Biochem. Biophys. 224: 169-177.
5. Arakawa, T., Timasheff, S. N. 1985. Mechanism of poly(ethylene glycol) interaction with proteins. Biochemistry 24: 6756.
6. Arakawa, T., Hsu, Y.-R., Yphantis, D. A. 1987. Acid unfolding and self-association of recombinant Escherichia coli delivered human interferon γ. Biochemistry 26: 5428-5432.
7. Arakawa, T., Hsu, Y.-R., Schiffer, S. G., Tsai, L. B., Curless, C., Fox, G. M. 1989. Characterization of cysteine-free analog of recombinant basic human fibroblast growth factor. Biochem. Biophys. Res. Commun. 161: 335-341.
8. Atha, D. H., Ingham, K. C. 1981. Mechanism of precipitation of proteins by polyethylene glycols. J. Biol. Chem. 256: 12108-12117.
9. Axen, R., Porath, J., Ernback, S. 1967. Chemical coupling of peptides and proteins to polysaccharides by means of cyanogen halides. Nature 214: 1302-1304.
10. Banerjee, S. K., Pogolotti, A. Jr., Rupley, J. A. 1975. Self-association of lysozyme. J. Biol. Chem. 250: 8260-8266.
11. Becker, G. W., Bowsher, R. R., Mackellar, W. C., Poor, M. L., Tackitt, P. M., Riggin, R. M. 1987. Chemical physical and biological characterization of biosynthetic human growth hormone. Biotech. Appl. Biochem. 9: 478-487.
12. Brange, J., Drejer, K., Hansen, J. F., Havelund, S., Kaarsholm, N. C., Melberg, S. G., Sorensen, A. R. 1989. Design of novel insulins with changed self-association and ligand binding properties. In: H. Blocker, J. Collins, R. D. Schmid, and D. Schomburg (eds.) Advances in Protein Design, International Workshop 1988. Chemie Weinheim, Basel, Switzerland.
13. Brems, D. N. 1988. Solubility of different folding conformers of bovine growth hormone. Biochemistry 27: 4541-4546.
14. Brems, D. N., Alter, L. A., Beckage, M. J., Chance, R. E., DiMarchi, R. D., Green, L. K., Long, H. B., Pekar, A. H., Shields, J. E., Frank, B. H. 1992. Altering the association properties of insulin by amino acid replacement. Protein Eng. 5: 527-533.
15. Brems, D. N., Brown, P. L., Bryant, C., Chance, R. E., DiMarchi, R. D., Green, K., Howey, D. C., Long, H. B., Miller, A. A., Millican, R., Pekar, A. M., Shields, J.E., Frank, B. H. 1993. Altering the self-association and stability of insulin by amino acid replacement. In: J. L. Cleland (ed.), Protein folding: In vivo and in vitro. American Chemical Society, Washington, DC.
16. Casal, H. L., Kohler, U., Mantsch, H. H. 1988. Structural and conformational changes of β-lactoglobulin B: An infrared spectroscopic study of the effect of pH and temperature. Biochim. Biophys. Acta 957: 11-20.
17. Chiancone, E., Fronticelli, C., Gattoni, M., Urbaitis, B., Bucci, E. 1992. Immobilized hemoglobin in the purification of hemoglobin-based oxygen carriers. J. Chromatogr. 604: 117-123.
18. Chou, P. Y., Fasman, G. D. 1974. Prediction of protein conformation. Biochemistry 19: 222-245.
19. Cleland, J. L., Powell, M. F., Shire, S. J. 1993. The development of stable protein formulations: A close look at protein aggregation, deamidation, and oxidation. Crit. Rev. Therapeut. Drug Carrier Sys. 10: 307-377.
20. Crosio, M., Janin, J., Jullien, M. 1992. Crystal packing in six crystal forms of pancreatic ribonuclease. J. Mol. Biol. 228: 243-251.
21. DeYoung, L. R., Fink, A. L., Dill, K. A. 1993. Aggregation and denaturation of apomyoglobin in aqueous urea solutions. Biochemistry 32: 3877-3886.
22. Dhal, P. K., Arnold, F. H. 1992. Metal-coordination interactions in the template-mediated synthesis of substrate-selective polymers: Recognition of bis(imidazole) substrates by copper(II) iminodiacetate containing polymers. Macromolecules 25: 7051-7059.
23. Diamond, R. 1974. Real-space refinement of the structure of hen-egg white lysozyme. J. Mol. Biol. 82: 371.
24. Fink, A. L., Calciano, L. J., Goto, Y., Kurotsu, T., Palleros, D. R. 1994. Classification of acid denaturation of proteins: Intermediates and unfolded states. Biochemistry 33: 12504-12511.
25. Fox, G. M., Schiffer, S. G., Rohde, M. F., Tsai, L. B., Banks, A. R., Arakawa, T. 1988. Production, biological activity, and structure of recombinant basic fibroblast growth factor and an analog with cysteine replaced by serine. J. Biol. Chem. 263: 18452-18458.
26. Gekko, K., Hasegawa Y. 1986. Compressibility-structure relationship of globular proteins. Biochemistry 25: 6563-6571.
27. Guilloteau, J., Ries-Kautt, M. M., Ducruix, A. F. 1992. Variation of lysozyme solubility as a function of temperature in the presence of organic and inorganic salts. J. Cryst. Growth 122: 223-230.
28. Guzov, V. M., Usanov, S. A., Chashchin, V. L. 1991. Immunoassay in the presence of water-soluble polymers. J. Immunol. Methods 145: 167-174.
29. Herzberg, O., Sussman, J. L. 1983. Protein model building by the use of a constrained-restrained least-squares procedure. J. Appl. Crystallogr. 16: 144.
30. Ingham, K. C. 1984. Protein precipitation with polyethylene glycol. Meth. Enz. 104: 351-356.
31. Ingram, V. M. 1959. Abnormal human haemoglobins. III. The chemical difference between normal and sickle haemoglobins. Biochim. Biophys. Acta. 36: 402-411.
32. Iyer, H. 1995. Ph.D. thesis, Rensselaer Polytechnic Institute, Troy, NY.
33. Jacobson, J., Frenz, J., Horvath, Cs. 1984. Measurement of adsorption isotherms by liquid chromatography. J. Chromatogr. 316: 53-68.
34. Jolles, P., Berthou, J. 1972. High temperature crystallization of lysozyme: An example of phase transition. FEBS Lett. 23: 21-23.
35. Kato, A. A., Takagi, T. J. 1988. Formation of intermolecular β-sheet structure during heat denaturation of ovalbumin. J. Agric. Food Chem. 38: 1156-1159.
36. Lee, J. C., Lee, L. L. Y. 1981. Preferential solvent interactions between proteins and polyethylene glycols. J. Biol. Chem. 256: 625.
37. Lewis, U. J., Cheever, E. V., Seavey, B. K. 1969a. Aggregate-free human growth hormone. I. Isolation by ultrafiltration. Endocrinology 84: 325-331.
38. Lewis, U. J., Parker, D. C., Okerlund, M. D., Boyar, R. M., Litteria, M., Vanderlaan, W. P. 1969b. Aggregate-free human growth hormone. II. Physico-chemical and biological properties. Endocrinology 84: 332-339.
39. McLean, M. A., Stayton, P. S., Sligar, S. G. 1993. Engineering protein orientation at surfaces to control macromolecular recognition events. Anal. Chem. 65: 2676-2678.
40. Melius, P., Wang, B.-C. 1974. Immobilization of lipase to cyanogen bromide activated polysaccharide carries. In: R. B. Dunlap, (ed.), Immobilized biochemicals and affinity chromatography. Plenum, New York.
41. Moore, W. V. Leppert, P. 1980. Role of aggregated human growth hormone (hGH) in development of antibodies to hGH. J. Clin. Endocrinol. 51: 691-697.
42. Oberg, K., Chrunyk, B. A., Wetzel, R., Fink, A. L. 1994. Nativelike secondary structure in interleukin-1-β inclusion bodies by attenuated total internal reflectance FTIR. Biochemistry 33: 2628-2634.
43. Pikal, M. J., Dellerman, K. M., Roy, M. L. 1991a. Formulation and stability of freeze-dried proteins: Effects of moisture and oxygen on the stability of freeze-dried formulations of human growth hormone. Dev. Biol. Stand. 74: 21.
44. Pikal, M. J., Dellerman, K. M., Roy, M. L., Riggin, R. M. 1991b. The effect of formulation variables on the stability of freeze-dried human growth hormone. Pharm. Res. 8: 427-436.
45. Pinckard, R. N., Weir, D. M., McBride, W. H. 1967. Factors influencing immune response. I. Effects of the physical state of the antigen and use of lymphoreticular cell proliferation on the response to intravenous injection of bovine serum albumin in rabbits. Clin. Exp. Immunol. 2: 331.
46. Pochapsky, T. C., Gopen, Q. 1992. A chromatographic approach to the determination of relative free energies of interaction between hydrophobic and amphiphilic amino acid side chains. Protein Sci. 1: 786-795.
47. Porath, J., Axen, R., Ernback, S. 1967. Chemical coupling of proteins to agarose. Nature 215: 1491-1492.
48. Przybycien, T. M., Bailey, J. E. 1989. Aggregation kinetics in salt-induced protein precipitation. AIChE J. 35: 1779-1790.
49. Przybycien, T. M., Bailey, J. E. 1991. Secondary structure perturbations in salt-induced protein precipitates. Biochim. Biophys. Acta 1076: 103-111.
50. Przybycien, T. M., Dunn, J. P., Valax, P., Georgiou, G. 1994. Secondary structure characterization of β-lactamase inclusion bodies. Prot. Eng. 7: 131-136.
51. Rao, S. T., Hogle, J., Sundaralingam, M. 1983. Studies of monoclinic hen egg white lysozyme. The refinement at 2.5 Å resolution: Conformational variability between the two independent molecules. Acta Crystallogr. 39: 237.
52. Robbins, D. C., Cooper, S. M., Fineberg, S. E., Mead, P. M. 1987. Antibodies to covalent aggregates of insulin in blood of insulin-using diabetic patients. Diabetes 36: 838.
53. Schellman, J. 1975. Macromolecular binding. Biopolymers 14: 999-1018.
54. Schellman, J. 1993. The relation between the free energy of interaction and binding. Biophys. Chem. 45: 273-279.
55. Sluzky, V., Tamada, J. A., Klibanov, A. M., Langer, R. 1992. Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces. Biotechnol. Bioeng. 40: 895-903.
56. Steinrauf, L. K. 1959. Preliminary X-ray data for some new crystalline forms of β-lactoglobulin and hen egg-white lysozyme. Acta Crystallogr. 12: 77-79.
57. Timasheff, S. N., Susi, H., Stevens. L. 1967. Infrared spectra and protein conformations in aqueous solutions. II. Survey of globular proteins. J. Biol. Chem. 242: 5467-5473.
58. Todd, R. J., Johnson, R. D., Arnold, F. H. 1994. Multiple-site binding interactions in metal-affinity chromatography. Equilibrium binding of engineered histidine-containing cytochromes c. J. Chrom. A 662: 13-26.
59. Waugh, D. F. 1944. The linkage of corpuscular protein molecules. I. A fibrous modification of insulin. J. Am. Chem. Soc. 66: 663.
60. Yeo, S.-D., Debenedetti, P. G., Patro, S. Y., Przybycien, T. M. 1994. Secondary structure characterization of microparticulate insulin powders. J. Pharm. Sci. 83: 1651-1656.