Protein instability during HIC: Describing the effects of mobile phase conditions on instability and chromatographic retention

Biotechnology and Bioengineering

Volumn 93, Issue 6, 2006, Pages 1177-1189

  Xiao, Yunzhi ^a   Freed, Alexander S ^a   Jones, Tara Tibbs ^a   Makrodimitris, Kostantinos ^a,b   O'Connell, John P ^a   Fernandez, Erik J ^a  

^a University of Virginia   (United States)

^b Whiting School of Engineering   (United States)

Author keywords

Alpha lactalbumin; Hydrogen deuterium isotope exchange; Hydrophobic interaction chromatography; Protein adsorption; Protein purification; Protein stability

Indexed keywords

ADSORPTION; AMMONIUM COMPOUNDS; HYDROPHOBIC CHROMATOGRAPHY; PHASE TRANSITIONS; SALTS;

ALPHA LACTALBUMIN; HYDROGEN-DEUTERIUM ISOTOPE EXCHANGE; HYDROPHOBIC INTERACTION CHROMATOGRAPHY; PROTEIN ADSORPTION; PROTEIN PURIFICATION; PROTEIN STABILITY;

PROTEINS;

ALPHA LACTALBUMIN;

ARTICLE; CHROMATOGRAPHY; MASS SPECTROMETRY; MATHEMATICAL ANALYSIS; PROTEIN DENATURATION; PROTEIN STABILITY; THERMODYNAMICS;

ADSORPTION; ALGORITHMS; AMMONIUM SULFATE; ANIMALS; CALCIUM; CATTLE; CHROMATOGRAPHY, GEL; COMPUTER SIMULATION; DEUTERIUM OXIDE; EDETIC ACID; HYDROPHOBICITY; LACTALBUMIN; MASS SPECTROMETRY; MODELS, THEORETICAL; PROTEIN DENATURATION; PROTEINS; SEPHAROSE; TEMPERATURE; THERMODYNAMICS; WATER;

EID: 33646052010     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.20826     Document Type: Article

References (40)

1. Bai Y, Milne JS, Mayne L, Englander SW. 1994. Protein stability parameters measured by hydrogen exchange. Proteins: Struct Funct Genet 20:4-14.
2. Benedek K, Dong S, Karger BL. 1984. Kinetics of unfolding of proteins on hydrophobic surfaces in reversed-phase liquid chromatography. J Chromatogr 317:227-243.
3. Carta G, Mahajan AJ, Cohen LM, Byers CH. 1992. Chromatography of reversibly reacting mixtures - mutarotation effects in sugar separations. Chem Eng Sci 47:1645-1657.
4. Engel MF, Visser AJ, van Mierlo CP. 2004. Conformation and orientation of a protein folding intermediate trapped by adsorption. Proc Natl Acad Sci USA 101:11316-11321.
5. Fausnaugh JL, Kennedy LA, Regnier FE. 1984. Comparison of hydrophobic-interaction and reversed-phase chromatography of proteins. J Chromatogr 317:141-155.
6. Forge V, Wijesinha RT, Balbach J, Brew K, Robinson CV, Redfield C, Dobson CM. 1999. Rapid collapse and slow structural reorganisation during the refolding of bovine alpha-lactalbumin. J Mol Biol 288:673-688.
7. Gagnon P, Grund E. 1996. Large-scale process development for hydrophobic interaction chromatography 4. Controlling selectivity. Biopharm 9:54-64.
8. Geng X, Regnier FE. 1984. Retention model for proteins in reversed-phase liquid chromatography. J Chromatogr 296:15-30.
9. Glasoe PK, Long FA. 1960. Use of glass electrodes to measure acidities in d2o. J Phys Chem 64:188-193.
10. Gloss LM, Placek BJ. 2002. The effect of salts on the stability of the h2a-h2b histone dimer. Biochemistry 41:14951-14959.
11. Hearn MTW, Hodder AN, Aguilar MI. 1985. High-performance liquid-chromatography of amino-acids, peptides and proteins.66. Investigations on the effects of chromatographic dwell in the reversed-phase high-performance liquid-chromatographic separation of proteins. J Chromatogr 327:47-66.
12. Hossain MM, Do DD. 1992. The effects of denaturation in the displacement chromatographic behaviour of proteins. Chem Eng J 49:B29-B39.
13. Ikeguchi M, Kuwajima K, Mitani M, Sugai S. 1986a. Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of alpha-lactalbumin and lysozyme. Biochemistry 25:6965-6972.
14. 2+-induced alteration in the unfolding behavior of alpha-lactalbumin. J Biochem (Tokyo) 99:1191-1201.
15. Jackson SE, Fersht aR. 1991. Folding of chymotrypsin inhibitor-2.2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition-state of folding. Biochemistry 30:10436-10443.
16. Jones TLT, Fernandez EJ. 2003. A-lactalbumin tertiary structure changes on hydrophobic interaction chromatography surfaces. J Colloid Interf Sci 259:27-35.
17. Jones TT, Fernandez EJ. 2004. Hydrophobic interaction chromatography selectivity changes among three stable proteins: Conformation does not play a major role. Biotech Bioeng 87:388-399.
18. Klinkenberg A. 1961. Chromatography of substances undergoing slow reversible chemical reactions. Chem Eng Sci 15:225-259.
19. Kuwajima K, Nitta K, Yoneyama M, Sugai S. 1976. Three-state denaturation of alpha-lactalbumin by guanidine hydrochloride. J Mol Biol 106:359-373.
20. Lee B, Richards FM. 1971. The interpretation of protein structures: Estimation of static accessibility. J Mol Biol 55:379-400.
21. Lindahl L, Vogel HJ. 1984. Metal-ion-dependent hydrophobic-interaction chromatography of alpha-lactalbumins. Anal Biochem 140:394-402.
22. McNay JL, Fernandez EJ. 1999. How does a protein unfold on a reversed-phase liquid chromatography surface? J Chromatogr A 849:135-148.
23. Melander W, Horvath C. 1977. Salt effect on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic series. Arch Biochem Biophys 183:200-215.
24. Melander WR, Lin H-J, Jacobson J, Horvath C. 1984. Dynamic effect of secondary equilibria in reversed-phase chromatography. J Phys Chem 88:4527-4536.
25. Myers JK, Pace CN, Scholtz JM. 1995. Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding. Protein Sci 4:2138-2148.
26. Oroszlan P, Blanco R, Lu XM, Yarmush D, Karger BL. 1990. Intrinsic fluorescence studies of the kinetic mechanism of unfolding of alpha-lactalbumin on weakly hydrophobic chromatographic surfaces. J Chromatogr 500:481-502.
27. Pace CN. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Meth Enzymol 131:266-280.
28. Pace CN. 1990. Measuring and increasing protein stability. Trends Biotechnol 8:93-98.
29. Perkins TW, Mak DS, Root TW, Lightfoot EN. 1997a. Protein retention in hydrophobic interaction chromatography: Modeling variation with buffer ionic strength and column hydrophobicity. J Chromatogr A 766:1-14.
30. Perkins TW, Root TW, Lightfoot EN. 1997b. Measuring column void volumes with nmr. Anal Chem 69:3293-3298.
31. Permyakov EA, Morozova LA, Burstein EA. 1985. Cation binding effects on the ph, thermal and urea denaturation transitions in alpha-lactalbumin. Biophys Chem 21:21-31.
32. Shukla AA, Peterson J, Sorge L, Lewis P, Thomas S, Waugh S. 2002. Preparative purification of a recombinant protein by hydrophobic interaction chromatography: Modulation of selectivity by the use of chaotropic additives. Biotechnol Prog 18:556-564.
33. Sokol JM, Holmes BH, O'Connell JP, Fernandez EJ. 2003. Aprotinin conformational distributions during reversed-phase liquid chromatography. Analysis by hydrogen-exchange mass spectrometry. J Chromatogr A 1007:55-66.
34. Staby A, Mollerup J. 1996. Solute retention of lysozyme in hydrophobic interaction perfusion chromatography. J Chromatogr A 734:205-212.
35. Tibbs Jones T. 2003. Using mass spectrometry to investigate protein-surface interactions during hydrophobic interaction chromatography. Ph.D. Diss., Chemical Engineering, University of Virginia, Charlottesville, VA. 155 p.
36. 2+ release. Biochemistry 35:16753-16759.
37. von Hippel PH, Wong K-Y. 1964. Neutral salts: The generality of their effects on the stability of macromolecular conformations. Science 145:577-580.
38. Wu SL, Benedek K, Karger BL. 1986a. Thermal behavior of proteins in high-performance hydrophobia-interaction chromatography. On-line spectroscopic and chromatographic characterization. J Chromatogr 359:3-17.
39. Wu SL, Figueroa A, Karger BL. 1986b. Protein conformational effects in hydrophobic interaction chromatography. Retention characterization and the role of mobile phase additives and stationary phase hydrophobicity. J Chromatogr 371:3-27.
40. Yang WY, Gruebele M. 2004. Rate-temperature relationships in lambda-repressor fragment lambda (6-85) folding. Biochemistry 43:13018-13025.