Prevention of thermal induced aggregation of cytochrome at isoelectric pH values by polyanions

Biotechnology and Bioengineering

Volumn 93, Issue 3, 2006, Pages 485-493

  Fedunová, Diana ^a   Antalík, Marián ^a,b  

^a INSTITUTE OF EXPERIMENTAL PHYSICS   (Slovakia)

^b P J AFÁRIK UNIVERSITY   (Slovakia)

Author keywords

Aggregation; Cytochrome c; Microcalorimetry; Polyanion; Thermal stability; Viscometry

Indexed keywords

AGGLOMERATION; DIFFERENTIAL SCANNING CALORIMETRY; NEGATIVE IONS; PH EFFECTS; PROTEINS; THERMODYNAMIC STABILITY; VISCOSITY MEASUREMENT;

CYTOCHROME C; ISOELECTRIC PH; MICROCALORIMETRY; POLYANION;

CHROMOSOMES;

CYTOCHROME C; POLYANION; POLYMER; POLYSTYRENESULFONIC ACID; POLYVINYL SULFATE; UNCLASSIFIED DRUG;

ARTICLE; CIRCULAR DICHROISM; COMPLEX FORMATION; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME STABILITY; HEAT; ISOELECTRIC POINT; MOLECULAR INTERACTION; PH; PROTEIN AGGREGATION; PROTEIN DENATURATION; VISCOMETRY;

CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; CYTOCHROMES C; HEAT; HYDROGEN-ION CONCENTRATION; POLYMERS; POLYVINYLS; SPECTROPHOTOMETRY, ULTRAVIOLET; SULFONIC ACIDS; VISCOSITY;

EID: 32644439994     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.20733     Document Type: Article

References (47)

1. Altamirano MM, Golbik R, Zahn R, Buckle AM, Fersht AR. 1997. Refolding chromatography with immobilized mini-chaperones. Proc Natl Acad Sci USA 94(8):3576-3578.
2. Aoki K, Taguchi H, Shindo Y, Yoshida M, Ogasahara K, Yutani K, Tanaka N. 1997. Calorimetric observation of a GroEL-protein binding reaction with little contribution of hydrophobic interaction. J Biol Chem 272: 32158-32162.
3. Arakawa T, Tsumoto K. 2003. The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation. Biochem Biophys Res Commun 304(1):148-152.
4. Austin C. 2003. Novel approach to obtain biologically active recombinant heterodimeric proteins in Escherichia coli. J Chromatogr B Analyt Technol Biomed Life Sci 786:93-107.
5. Bágel'ová J, Antalík M, Bona M. 1994. Studies on cytochrome c-heparin interactions by differential scanning calorimetry. Biochem J 297:99-101.
6. Bánó M, Strhársky I, Hrmo I. 2003. A viscosity and density meter with a magnetically suspended rotor. Rev Sci Instrum 74:4788-4793.
7. Benditt E, Cohen A, Franklin E, Glenner G, Husby G. 1980. Amyloid and Amyloidosis. Int Congr Ser No. 497. New York: Elsevier.
8. Bondos SE, Bicknell A. 2003. Detection and prevention of protein aggregation before, during, and after purification. Anal Biochem 316:223-231.
9. Brown LR, Deng J, Noll DM, Mori N, Clarke ND. 1997. Construction and overexpression of a synthetic gene for human DNA methylguanine methyltransferase: Renaturation and rapid purification of the protein. Protein Expr Purif 9:337-345.
10. Buchner J, Rudolph R. 1991. Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli. Biotechnology (NY) 9(2):157-162.
11. De Felice FG, Ferreira ST. 2002. Beta-amyloid production, aggregation, and clearance as targets for therapy in Alzheimer's disease. Cell Mol Neurobiol 22(5-6):545-563.
12. Fink AL. Chaperone-mediated protein folding. 1999 Physiol Rev 79(2):425-449.
13. Goldberg ME, Zetina CR. 1980. In: Jaenicke R. editor. Protein folding. Amsterdam and New York: Elsevier/North-Holland Biomedical Press. pp 469-484.
14. Hartl FU, Hayer-Hartl M. 2002. Molecular chaperones in the cytosol: From nascent chain to folded protein. Science 295(5561):1852-1858.
15. Herr AB, Ornitz DM, Sasisekharan R, Venkatamaran G, Waksman G. 1997. Heparin-induced self-association of fibroblast growth factor-2. Evidence for two oligomerization processes. J Biol Chem 272:6382-16389.
16. Hildebrandt P. 1990. Polyanion binding to cytochrome c probed by resonance Raman spectroscopy. Biochim Biophys Acta 1040:175-186.
17. Hildebrandt P, Stockburger M. 1989a. Cytochrome c at charged interfaces 1. Conformational and redox eauilibria at the electrode/electrolyte interface probed by surface-enhanced resonsance raman spectroscopy. Biochemistry 28:6710-6721.
18. Hildebrandt P, Stockburger M. 1989b. Cytochrome c at charged interfaces 2. Complexes with negatively charged macromolecular systems studied by resonance raman spectroscopy. Biochemistry 28:6722-6728.
19. Hildebrandt P, Heimburg T, Marsh D, Powell GL. 1990. Confornational changes in cytochrome c and cytochrome oxidase upon complex formation: A Resonance Raman Study. Biochemistry 29:1661-1668.
20. Honda C, Kamizono H, Samejima T, Endo K. 2000. Studies on thermal aggregation of bovine serum albumin as a drug carrier. Chem Pharm Bull (Tokyo) 48(4):464-466.
21. Hoyer W, Cherny D, Subramaniam V, Jovin TM. 2004. Impact of the acidic C-terminal region comprising amino acids 109-140 on alpha-synuclein aggregation in vitro. Biochemistry 43(51):16233-16242.
22. Joly M. 1965. A physicochemical approach to the denaturation of proteins. New York: Academic Press, pp. 153-170.
23. Kosinski-Collins MS, King J. 2003. In vitro unfolding, refolding, and polymerization of human gammaD crystallin, a protein involved in cataract formation. Protein Sci 12(3):480-490.
24. Kudou M, Shiraki K, Fujiwara S, Imanaka T, Takagi M. 2003. Prevention of thermal inactivation and aggregation of lysozyme by polyamines. Eur J Biochem 270(22):4547-4554.
25. Kurganov BI. 2002. Kinetics of protein aggregation. Quantitative estimation of the chaperone-like activity in test-systems based on suppression of protein aggregation. Biochemistry (Mosc) 67(4):409-422.
26. Lohner K, Esser AF. 1991. Thermal unfolding and aggregation of human complement protein C9: a differential scanning calorimetry study. Biochemistry 2;30(26):6620-6625.
27. Matthews JM, Ward LD, Hammacher A, Norton RS, Simpson RJ. 1997. Roles of histidine 31 and tryptophan 34 in the structure, self-association, and folding of murine interleukin-6. Biochemistry 36:6187-6196.
28. Moy FJ, Safran M, Seddon AP, Kitchen D, Bohlen P, Aviezer D, Yayon A, Powers R. 1997. Properly oriented heparin-decasaccharide-induced dimers are the biologically active form of basic fibroblast growth factor. Biochemistry 36:4782-4791.
29. Muga A, Mantsch HH, Surewicz WK. 1991. Membrane binding induces destabilization of cytochrome c structure. Biochemistry 30(29):7219-7224.
30. Muronetz VI, Kazakov SV, Dainiak MB, Izumrudov VA, Galaev IY, Mattiasson B. 2000. Calorimetric observation of a GroEL-protein binding reaction with little contribution of hydrophobic interaction. Biochim Biophys Acta 1475:141-150.
31. Privalov L, Khechinashvili NN. 1974. A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study. J Mol Biol 86:665-684.
32. Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH. 1997. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90:65-75.
33. Rentzeperis D, Jonsson T, Sauer RT. 1999. Acceleration of the refolding of Arc repressor by nucleic acids and other polyanions. Nature Struct Biol 6:569-573.
34. Rozema D, Gellman SH. 1996. Artificial chaperone-assisted refolding of denatured-reduced lysozyme: modulation of the competition between renaturation and aggregation. Biochemistry 35(49):15760-15771.
35. Rudolph R, Lilie H. 1996. In vitro folding of inclusion body proteins. FASEB J. 10(1):49-56.
36. Sedlák E, Antalík M. 1998. Coulombic and noncoulombic effect of polyanions on cytochrome c structure. Biopolymers 46:145-154.
37. Sedlák E, Antalík M. 1999. Molten globule-like state of cytochrome c induced by polyanion poly(vinylsulfate) in slightly acidic pH. Biochim Biophys Acta 1434:347-355.
38. Shastry BS. 2003. Neurodegenerative disorders of protein aggregation. Neurochem Int. 43(1):1-7.
39. Shrake A, Ross PD. 1992. Origins and consequences of ligand-induced multiphasic thermal protein denaturation. Biopolymers 32:925-940.
40. Taneja S, Ahmad F. 1994. Increased thermal stability of proteins in the presence of amino acids. Biochem J 303 (Pt 1):147-153.
41. Tsai AM, van Zanten JH, Betenbaugh MJ. 1998a. I. Study of protein aggregation due to heat denaturation: A structural approach using circular dichroism spectroscopy, nuclear magnetic resonance, and static light scattering. Biotechnol Bioeng 59:273-280.
42. Tsai AM, van Zanten JH, Betenbaugh MJ. 1998b. II. Electrostatic effect in the aggregation of heat-denatured RNase A and implications for protein additive design. Biotechnol Bioeng 59:281-285.
43. Van Montfort R, Slingsby C, Vierling E. 2001. Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones. Adv Protein Chem 59:105-156.
44. Villaverde A, Carrio MM. 2003. Protein aggregation in recombinant bacteria: biological role of inclusion bodies. Biotechnol Lett 25(17): 1385-1395.
45. Wadsworth JD, Hill AF, Beck JA, Collinge J. 2003. Molecular and clinical classification of human prion disease. Br Med Bull 66:241-254.
46. Waksman G, Herr AB. 1998. New insights into heparin-induced FGF oligomerization. Nature Struct Biol 5:527-530.
47. Weijers M, Barneveld PA, Cohen Stuart MA, Visschers RW. 2003. Heat-induced denaturation and aggregation of ovalbumin at neutral pH described by irreversible first-order kinetics. Protein Sci 12(12):2693-2703.