메뉴 건너뛰기




Volumn 67, Issue 2, 2007, Pages 309-319

Solution formulation and lyophilisation of a recombinant fibronectin fragment

Author keywords

Calorimetry; Cell adhesion; Circular dichroism; Fibronectin; Formulation; Thermal stability

Indexed keywords

FIBRONECTIN; FIBRONECTIN TYPE III; GUANIDINE; MACROGOL 6000; RECOMBINANT FIBRONECTIN; SUCROSE; UNCLASSIFIED DRUG; VASCULAR TARGETING AGENT;

EID: 34547697312     PISSN: 09396411     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejpb.2007.03.009     Document Type: Article
Times cited : (11)

References (31)
  • 1
    • 0028346713 scopus 로고
    • The role of the ninth and tenth type III domains of human fibronectin in cell adhesion
    • Mardon H.J., and Grant K.E. The role of the ninth and tenth type III domains of human fibronectin in cell adhesion. FEBS Lett. 340 (1994) 197-201
    • (1994) FEBS Lett. , vol.340 , pp. 197-201
    • Mardon, H.J.1    Grant, K.E.2
  • 2
    • 0037404371 scopus 로고    scopus 로고
    • Engineering cell adhesive surfaces that direct integrin alpha5beta1 binding using a recombinant fragment of fibronectin
    • Cutler S.M., and Garcia A.J. Engineering cell adhesive surfaces that direct integrin alpha5beta1 binding using a recombinant fragment of fibronectin. Biomaterials 24 (2003) 1759-1770
    • (2003) Biomaterials , vol.24 , pp. 1759-1770
    • Cutler, S.M.1    Garcia, A.J.2
  • 3
    • 0033843942 scopus 로고    scopus 로고
    • Regulation of angiogenesis in vivo by ligation of integrin alpha5beta1 with the central cell-binding domain of fibronectin
    • Kim S., Bell K., Mousa S.A., and Varner J.A. Regulation of angiogenesis in vivo by ligation of integrin alpha5beta1 with the central cell-binding domain of fibronectin. Am. J. Pathol. 156 (2000) 1345-1362
    • (2000) Am. J. Pathol. , vol.156 , pp. 1345-1362
    • Kim, S.1    Bell, K.2    Mousa, S.A.3    Varner, J.A.4
  • 4
    • 0032982248 scopus 로고    scopus 로고
    • Development of cytotrophoblast columns from explanted first-trimester human placental villi: role of fibronectin and integrin alpha5beta1
    • Aplin J.D., Haigh T., Jones C.J., Church H.J., and Vicovac L. Development of cytotrophoblast columns from explanted first-trimester human placental villi: role of fibronectin and integrin alpha5beta1. Biol. Reprod. 60 (1999) 828-838
    • (1999) Biol. Reprod. , vol.60 , pp. 828-838
    • Aplin, J.D.1    Haigh, T.2    Jones, C.J.3    Church, H.J.4    Vicovac, L.5
  • 5
    • 0036941808 scopus 로고    scopus 로고
    • Novel mutant human fibronectin FIII9-10 domain pair with increased conformational stability and biological activity
    • van der Walle C.F., Altroff H., and Mardon H.J. Novel mutant human fibronectin FIII9-10 domain pair with increased conformational stability and biological activity. Protein Eng. 15 (2002) 1021-1024
    • (2002) Protein Eng. , vol.15 , pp. 1021-1024
    • van der Walle, C.F.1    Altroff, H.2    Mardon, H.J.3
  • 6
    • 0030725266 scopus 로고    scopus 로고
    • Preferential exclusion of sucrose from recombinant interleukin-1 receptor antagonist: role in restricted conformational mobility and compaction of native state
    • Kendrick B.S., Chang B.S., Arakawa T., Peterson B., Randolph T.W., Manning M.C., and Carpenter J.F. 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 (1997) 11917-11922
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11917-11922
    • Kendrick, B.S.1    Chang, B.S.2    Arakawa, T.3    Peterson, B.4    Randolph, T.W.5    Manning, M.C.6    Carpenter, J.F.7
  • 7
    • 0019888281 scopus 로고
    • The stabilization of proteins by sucrose
    • Lee J.C., and Timasheff S.N. The stabilization of proteins by sucrose. J. Biol. Chem. 256 (1981) 7193-7201
    • (1981) J. Biol. Chem. , vol.256 , pp. 7193-7201
    • Lee, J.C.1    Timasheff, S.N.2
  • 8
    • 0033562141 scopus 로고    scopus 로고
    • Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding
    • Allison S.D., Chang B., Randolph T.W., and Carpenter J.F. Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding. Arch. Biochem. Biophys. 365 (1999) 289-298
    • (1999) Arch. Biochem. Biophys. , vol.365 , pp. 289-298
    • Allison, S.D.1    Chang, B.2    Randolph, T.W.3    Carpenter, J.F.4
  • 9
    • 0032782071 scopus 로고    scopus 로고
    • Instability, stabilization, and formulation of liquid protein pharmaceuticals
    • Wang W. Instability, stabilization, and formulation of liquid protein pharmaceuticals. Int. J. Pharm. 185 (1999) 129-188
    • (1999) Int. J. Pharm. , vol.185 , pp. 129-188
    • Wang, W.1
  • 11
    • 0032949245 scopus 로고    scopus 로고
    • A central composite design to investigate the thermal stabilization of lysozyme
    • Branchu S., Forbes R.T., York P., and Nyqvist H. A central composite design to investigate the thermal stabilization of lysozyme. Pharm. Res. 16 (1999) 702-708
    • (1999) Pharm. Res. , vol.16 , pp. 702-708
    • Branchu, S.1    Forbes, R.T.2    York, P.3    Nyqvist, H.4
  • 12
    • 0037452426 scopus 로고    scopus 로고
    • New approach to stability assessment of protein solution formulations by differential scanning calorimetry
    • Cueto M., Dorta M.J., Munguia O., and Llabres M. New approach to stability assessment of protein solution formulations by differential scanning calorimetry. Int. J. Pharm. 252 (2003) 159-166
    • (2003) Int. J. Pharm. , vol.252 , pp. 159-166
    • Cueto, M.1    Dorta, M.J.2    Munguia, O.3    Llabres, M.4
  • 13
    • 0035079183 scopus 로고    scopus 로고
    • Thermal and urea-induced unfolding in T7 RNA polymerase: calorimetry, circular dichroism and fluorescence study
    • Griko Y., Sreerama N., Osumi-Davis P., Woody R.W., and Woody A.Y. Thermal and urea-induced unfolding in T7 RNA polymerase: calorimetry, circular dichroism and fluorescence study. Protein Sci. 10 (2001) 845-853
    • (2001) Protein Sci. , vol.10 , pp. 845-853
    • Griko, Y.1    Sreerama, N.2    Osumi-Davis, P.3    Woody, R.W.4    Woody, A.Y.5
  • 14
    • 13144250209 scopus 로고    scopus 로고
    • Solution structure and dynamics of linked cell attachment modules of mouse fibronectin containing the RGD and synergy regions: comparison with the human fibronectin crystal structure
    • Copie V., Tomita Y., Akiyama S.K., Aota S., Yamada K.M., Venable R.M., Pastor R.W., Krueger S., and Torchia D.A. Solution structure and dynamics of linked cell attachment modules of mouse fibronectin containing the RGD and synergy regions: comparison with the human fibronectin crystal structure. J. Mol. Biol. 277 (1998) 663-682
    • (1998) J. Mol. Biol. , vol.277 , pp. 663-682
    • Copie, V.1    Tomita, Y.2    Akiyama, S.K.3    Aota, S.4    Yamada, K.M.5    Venable, R.M.6    Pastor, R.W.7    Krueger, S.8    Torchia, D.A.9
  • 15
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy D.J., Aukhil I., and Erickson H.P. 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 84 (1996) 155-164
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 16
    • 0023661027 scopus 로고
    • Vacuum ultraviolet circular dichroism of fibronectin. Dominant tyrosine effects
    • Stevens E.S., Morris E.R., Charlton J.A., and Rees D.A. Vacuum ultraviolet circular dichroism of fibronectin. Dominant tyrosine effects. J. Mol. Biol. 197 (1987) 743-745
    • (1987) J. Mol. Biol. , vol.197 , pp. 743-745
    • Stevens, E.S.1    Morris, E.R.2    Charlton, J.A.3    Rees, D.A.4
  • 17
    • 0024593759 scopus 로고
    • On the origin of the positive band in the far-ultraviolet circular dichroic spectrum of fibronectin
    • Khan M.Y., Villanueva G., and Newman S.A. On the origin of the positive band in the far-ultraviolet circular dichroic spectrum of fibronectin. J. Biol. Chem. 264 (1989) 2139-2142
    • (1989) J. Biol. Chem. , vol.264 , pp. 2139-2142
    • Khan, M.Y.1    Villanueva, G.2    Newman, S.A.3
  • 18
    • 0034255393 scopus 로고    scopus 로고
    • Lyophilization and development of solid protein pharmaceuticals
    • Wang W. Lyophilization and development of solid protein pharmaceuticals. Int. J. Pharm. 203 (2000) 1-60
    • (2000) Int. J. Pharm. , vol.203 , pp. 1-60
    • Wang, W.1
  • 19
    • 1242314686 scopus 로고    scopus 로고
    • Design of freeze-drying processes for pharmaceuticals: practical advice
    • Tang X.L., and Pikal M.J. Design of freeze-drying processes for pharmaceuticals: practical advice. Pharm. Res. 21 (2004) 191-200
    • (2004) Pharm. Res. , vol.21 , pp. 191-200
    • Tang, X.L.1    Pikal, M.J.2
  • 20
    • 25444466477 scopus 로고    scopus 로고
    • Thermodynamic and dynamic factors involved in the stability of native protein structure in amorphous solids in relation to levels of hydration
    • Hill J.J., Shalaev E.Y., and Zografi G. Thermodynamic and dynamic factors involved in the stability of native protein structure in amorphous solids in relation to levels of hydration. J. Pharm. Sci. 94 (2005) 1636-1667
    • (2005) J. Pharm. Sci. , vol.94 , pp. 1636-1667
    • Hill, J.J.1    Shalaev, E.Y.2    Zografi, G.3
  • 21
    • 23844447975 scopus 로고    scopus 로고
    • Mechanism of protein stabilization by sugars during freeze-drying and storage: native structure preservation, specific interaction, and/or immobilization in a glassy matrix?
    • Chang L.Q., Shepherd D., Sun J., Ouellette D., Grant K.L., Tang X.L., and Pikal M.J. Mechanism of protein stabilization by sugars during freeze-drying and storage: native structure preservation, specific interaction, and/or immobilization in a glassy matrix?. J. Pharm. Sci. 94 (2005) 1427-1444
    • (2005) J. Pharm. Sci. , vol.94 , pp. 1427-1444
    • Chang, L.Q.1    Shepherd, D.2    Sun, J.3    Ouellette, D.4    Grant, K.L.5    Tang, X.L.6    Pikal, M.J.7
  • 22
    • 33845680820 scopus 로고    scopus 로고
    • Emulsifying performance of modular {beta}-sandwich proteins: the hydrophobic moment and conformational stability
    • Annan W.S., Fairhead M., Pereira P., and van der Walle C.F. Emulsifying performance of modular {beta}-sandwich proteins: the hydrophobic moment and conformational stability. Protein Eng. Des. Sel. 19 (2006) 537-545
    • (2006) Protein Eng. Des. Sel. , vol.19 , pp. 537-545
    • Annan, W.S.1    Fairhead, M.2    Pereira, P.3    van der Walle, C.F.4
  • 23
    • 11244284850 scopus 로고    scopus 로고
    • Interdomain tilt angle determines integrin-dependent function of the ninth and tenth FIII domains of human fibronectin
    • Altroff H., Schlinkert R., van der Walle C.F., Bernini A., Campbell I.D., Werner J.M., and Mardon H.J. Interdomain tilt angle determines integrin-dependent function of the ninth and tenth FIII domains of human fibronectin. J. Biol. Chem. 279 (2004) 55995-56003
    • (2004) J. Biol. Chem. , vol.279 , pp. 55995-56003
    • Altroff, H.1    Schlinkert, R.2    van der Walle, C.F.3    Bernini, A.4    Campbell, I.D.5    Werner, J.M.6    Mardon, H.J.7
  • 24
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher M.D., and Ruoslahti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 309 (1984) 30-33
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 25
    • 0031556949 scopus 로고    scopus 로고
    • Module-module interactions in the cell binding region of fibronectin: stability, flexibility and specificity
    • Spitzfaden C., Grant R.P., Mardon H.J., and Campbell I.D. Module-module interactions in the cell binding region of fibronectin: stability, flexibility and specificity. J. Mol. Biol. 265 (1997) 565-579
    • (1997) J. Mol. Biol. , vol.265 , pp. 565-579
    • Spitzfaden, C.1    Grant, R.P.2    Mardon, H.J.3    Campbell, I.D.4
  • 26
    • 0031214363 scopus 로고    scopus 로고
    • A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules
    • Plaxco K.W., Spitzfaden C., Campbell I.D., and Dobson C.M. A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules. J. Mol. Biol. 270 (1997) 763-770
    • (1997) J. Mol. Biol. , vol.270 , pp. 763-770
    • Plaxco, K.W.1    Spitzfaden, C.2    Campbell, I.D.3    Dobson, C.M.4
  • 28
    • 0001002352 scopus 로고
    • Conformation changes of proteins
    • Lumry R., and Eyring H. Conformation changes of proteins. J. Phys. Chem. 58 (1954) 110-120
    • (1954) J. Phys. Chem. , vol.58 , pp. 110-120
    • Lumry, R.1    Eyring, H.2
  • 29
    • 0141560454 scopus 로고    scopus 로고
    • The 'glass transition' in protein dynamics: what it is, why it occurs, and how to exploit it
    • Ringe D., and Petsko G.A. The 'glass transition' in protein dynamics: what it is, why it occurs, and how to exploit it. Biophys. Chem. 105 (2003) 667-680
    • (2003) Biophys. Chem. , vol.105 , pp. 667-680
    • Ringe, D.1    Petsko, G.A.2
  • 30
    • 0001498936 scopus 로고
    • Solid aqueous-solutions
    • Franks F. Solid aqueous-solutions. Pure Appl. Chem. 65 (1993) 2527-2537
    • (1993) Pure Appl. Chem. , vol.65 , pp. 2527-2537
    • Franks, F.1
  • 31
    • 0035914421 scopus 로고    scopus 로고
    • The eighth FIII domain of human fibronectin promotes integrin alpha5beta1 binding via stabilization of the ninth FIII domain
    • Altroff H., van der Walle C.F., Asselin J., Fairless R., Campbell I.D., and Mardon H.J. The eighth FIII domain of human fibronectin promotes integrin alpha5beta1 binding via stabilization of the ninth FIII domain. J. Biol. Chem. 276 (2001) 38885-38892
    • (2001) J. Biol. Chem. , vol.276 , pp. 38885-38892
    • Altroff, H.1    van der Walle, C.F.2    Asselin, J.3    Fairless, R.4    Campbell, I.D.5    Mardon, H.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.