Effects of solutes on empirical phase diagrams of human fibroblast growth factor 1

Journal of Pharmaceutical Sciences

Volumn 96, Issue 6, 2007, Pages 1490-1503

  Fan, Haihong ^a   Li, Huaina ^b   Zhang, Mingyu ^b   Russell Middaugh, C ^a  

^a UNIVERSITY OF KANSAS   (United States)

^b Phage Biotechnology Corporation   (United States)

Author keywords

Circular dichroism; Excipients; Fluorescence spectroscopy; Physical characterization; UV Vis spectroscopy

Indexed keywords

HEPARIN; RECOMBINANT FIBROBLAST GROWTH FACTOR 1; RECOMBINANT GROWTH FACTOR; SUCROSE; UNCLASSIFIED DRUG;

ARTICLE; CIRCULAR DICHROISM; DRUG FORMULATION; FLUORESCENCE SPECTROSCOPY; LOW TEMPERATURE; PH; PROTEIN AGGREGATION; PROTEIN STABILITY; PROTEIN STRUCTURE; SOLUTE; THERMOSTABILITY; ULTRAVIOLET SPECTROSCOPY;

EID: 34250703143     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.20796     Document Type: Article

References (46)

1. Pavlou AK, Reichert JM. 2004. Recombinant protein therapeutics - success rates, market trends and values to 2010. Nat Biotechnol 22:1513-1519.
2. Volkin DB, Sanyal G, Burke CJ, Middaugh CR. 2002. Preformulation studies as an essential guide to formulation development and manufacture of protein pharmaceuticals. Pharm Biotechnol 14:1-46.
3. Kueltzo LA, Ersoy B, Ralston JP, Middaugh CR. 2003. Derivative absorbance spectroscopy and protein phase diagrams as tools for comprehensive protein characterization: A bGCSF case study. J Pharm Sci 92:1805-1820.
4. Fan H, Ralston J, Dibiase M, Faulkner E, Russell Middaugh C. 2005. Solution behavior of IFN-beta-1a: An empirical phase diagram based approach. J Pharm Sci 94:1893-1911.
5. Jiang G, Joshi SB, Peek LJ, Brandau DT, Huang J, Ferriter MS, Woodley WD, Ford BM, Mar KD, Mikszta JA, Hwang CR, Ulrich R, Harvey NG, Middaugh CR, Sullivan VJ. 2006. Anthrax vaccine powder formulations for nasal mucosal delivery. J Pharm Sci 95:80-96.
6. Fan H, Kashi RS, Middaugh CR. 2006. Conformational lability of two molecular chaperones Hsc70 and gp96: Effects of pH and temperature. Arch Biochem Biophys 447:34-45.
7. Ausar SF, Rexroad J, Frolov VG, Look JL, Konar N, Middaugh CR. 2005. Analysis of the thermal and pH stability of human respiratory syncytial virus. Mol Pharm 2:491-499.
8. Rexroad J, Evans RK, Middaugh CR. 2006. Effect of pH and ionic strength on the physical stability of adenovirus type 5. J Pharm Sci 95:237-247.
9. Manning MC, Patel K, Borchardt RT. 1989. Stability of protein pharmaceuticals. Pharm Res 6:903-918.
10. Volkin DB, Mach H, Middaugh CR. 1997. Degradative covalent reactions important to protein stability. Mol Biotechnol 8:105-122.
11. Wang W. 1999. Instability, stabilization, and formulation of liquid protein pharmaceuticals. Int J Pharm 185:129-188.
12. Frokjaer S, Otzen DE. 2005. Protein drug stability: A formulation challenge. Nat Rev Drug Discov 4:298-306.
13. Timasheff SN. 1993. The control of protein stability and association by weak interactions with water: How do solvents affect these processes? Annu Rev Biophys Biomol Struct 22:67-97.
14. Timasheff SN. 1998. Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated. Adv Protein Chem 51:355-432.
15. Kendrick BS, Li T, Chang BS. 2002. Physical stabilization of proteins in aqueous solution. Pharm Biotechnol 13:61-84.
16. Lee JC, Timasheff SN. 1981. The stabilization of proteins by sucrose. J Biol Chem 256:7193-7201.
17. Liu Y, Bolen DW. 1995. The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes. Biochemistry 34:12884-12891.
18. Kendrick BS, Chang BS, Arakawa T, Peterson B, Randolph TW, Manning MC, Carpenter JF. 1997. Preferential exclusion of sucrose from recombinant interleukin-1 receptor antagonist: Role in restricted conformational mobility and compaction of native state. Proc Natl Acad Sci USA 94:11917-11922.
19. Kretschmar M, Mayr EM, Jaenicke R. 1999. Kinetic and thermodynamic stabilization of the betagamma-crystallin homolog spherulin 3a from Physarum polycephalum by calcium binding. J Mol Biol 289:701-705.
20. Blaber M, DiSalvo J, Thomas KA. 1996. X-ray crystal structure of human acidic fibroblast growth factor. Biochemistry 35:2086-2094.
21. Bernett MJ, Somasundaram T, Blaber M. 2004. An atomic resolution structure for human fibroblast growth factor 1. Proteins 57:626-634.
22. Murzin AG, Lesk AM, Chothia C. 1992. beta-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1 beta and 1 alpha and fibroblast growth factors. J Mol Biol 223:531-543.
23. Imamura T, Friedman SA, Gamble S, Tokita Y, Opalenik SR, Thompson JA, Maciag T. 1995. Identification of the domain within fibroblast growth factor-1 responsible for heparin-dependence. Biochim Biophys Acta 1266:124-130.
24. DiGabriele AD, Lax I, Chen DI, Svahn CM, Jaye M, Schlessinger J, Hendrickson WA. 1998. Structure of a heparin-linked biologically active dimer of fibroblast growth factor. Nature 393:812-817.
25. Ortega S, Schaeffer MT, Soderman D, DiSalvo J, Linemeyer DL, Gimenez-Gallego G, Thomas KA. 1991. Conversion of cysteine to serine residues alters the activity, stability, and heparin dependence of acidic fibroblast growth factor. J Biol Chem 266:5842-5846.
26. Klagsbrun M. 1989. The fibroblast growth factor family: Structural and biological properties. Prog Growth Factor Res 1:207-235.
27. Middaugh CR, Volkin DB, Thomas KA. 1993. Acidic and basic fibroblast growth factors. Curr Opin Invest Drugs 2:991-1005.
28. Volkin DB, Middaugh CR. 1996. The characterization, stabilization, and formulation of acidic fibroblast growth factor. Pharm Biotechnol 9:181-217.
29. Volkin DB, Tsai PK, Dabora JM, Gress JO, Burke CJ, Linhardt RJ, Middaugh CR. 1993. Physical stabilization of acidic fibroblast growth factor by polyanions. Arch Biochem Biophys 300:30-41.
30. Tsai PK, Volkin DB, Dabora JM, Thompson KC, Bruner MW, Gress JO, Matuszewska B, Keogan M, Bondi JV, Middaugh CR. 1993. Formulation design of acidic fibroblast growth factor. Pharm Res 10: 649-659.
31. Copeland RA, Ji H, Halfpenny AJ, Williams RW, Thompson KC, Herber WK, Thomas KA, Bruner MW, Ryan JA, Marquis-Omer D, et al. 1991. The structure of human acidic fibroblast growth factor and its interaction with heparin. Arch Biochem Biophys 289:53-61.
32. Srimathi T, Kumar TK, Kathir KM, Chi YH, Srisailam S, Lin WY, Chiu IM, Yu C. 2003. Structurally homologous all beta-barrel proteins adopt different mechanisms of folding. Biophys J 85:459-472.
33. Venyaminov SY, Yang JT. 1996. Determination of protein secondary structure. In: Fasman GD, editor. Circular dichroism and the conformational analysis of biomolecules, 1st ed., New York: Plenum Press. pp 69-109.
34. Woody RW, Dunker AK. 1996. Aromatic and cystine side-chain circular dichroism in proteins. In: Fasman GD, editor. Circular dichroism and the conformational analysis of biomolecules, 1st ed., New York: Plenum Press. pp 109-158.
35. Mach H, Middaugh CR. 1995. Interaction of partially structured states of acidic fibroblast growth factor with phospholipid membranes. Biochemistry 34:9913-9920.
36. Pineda-Lucena A, Nunez De Castro I, Lozano RM, Munoz-Willery I, Zazo M, Gimenez-Gallego G. 1994. Effect of low pH and heparin on the structure of acidic fibroblast growth factor. Eur J Biochem 222:425-431.
37. Semisotnov GV, Rodionova NA, Razgulyaev OI, Uversky VN, Gripas AF, Gilmanshin RI. 1991. Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers 31:119-128.
38. Matulis D, Lovrien R. 1998. 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation. Biophys J 74:422-429.
39. Mazon H, Marcillat O, Forest E, Smith DL, Vial C. 2004. Conformational dynamics of the GdmHCl-induced molten globule state of creatine kinase monitored by hydrogen exchange and mass spectrometry. Biochemistry 43:5045-5054.
40. Almstedt K, Lundqvist M, Carlsson J, Karlsson M, Persson B, Jonsson BH, Carlsson U, Hammarstrom P. 2004. Unfolding a folding disease: Folding, misfolding and aggregation of the marble brain syndrome-associated mutant H107Y of human carbonic anhydrase II. J Mol Biol 342:619-633.
41. Mach H, Middaugh CR. 1994. Simultaneous monitoring of the environment of tryptophan, tyrosine, and phenylalanine residues in proteins by near-ultraviolet second-derivative spectroscopy. Anal Biochem 222:323-331.
42. Mach H, Volkin DB, Burke CJ, Middaugh CR. 1995. Ultraviolet absorption spectroscopy. Methods Mol Biol 40:91-114.
43. Gospodarowicz D, Cheng J. 1986. Heparin protects basic and acidic FGF from inactivation. J Cell Physiol 128:475-484.
44. Rosengart TK, Johnson WV, Friesel R, Clark R, Maciag T. 1988. Heparin protects heparin-binding growth factor-I from proteolytic inactivation in vitro. Biochem Biophys Res Commun 152:432-440.
45. Linemeyer DL, Menke JG, Kelly LJ, DiSalvo J, Soderman D, Schaeffer MT, Ortega S, Gimenez-Gallego G, Thomas KA. 1990. Disulfide bonds are neither required, present, nor compatible with full activity of human recombinant acidic fibroblast growth factor. Growth Factors 3:287-298.
46. Edwards KL, Kueltzo LA, Fisher MT, Middaugh CR. 2001. Complex effects of molecular chaperones on the aggregation and refolding of fibroblast growth factor-1. Arch Biochem Biophys 393:14-21.