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Volumn 23, Issue 1, 2006, Pages 148-155

Kinetics of insulin adsorption at the oil-water interface and diffusion properties of adsorbed layers monitored using fluorescence correlation spectroscopy

Author keywords

Adsorption; Fluorescence; Fluorescence correlation spectroscopy; Insulin; Oil water interface

Indexed keywords

RECOMBINANT HUMAN INSULIN;

EID: 32244435209     PISSN: 07248741     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11095-005-8636-3     Document Type: Article
Times cited : (18)

References (41)
  • 2
    • 0029251458 scopus 로고
    • Structures and stabilities of adsorbed proteins
    • C. A. Haynes W. Norde 1995 Structures and stabilities of adsorbed proteins J. Colloid Interface Sci. 169 313 328
    • (1995) J. Colloid Interface Sci. , vol.169 , pp. 313-328
    • Haynes, C.A.1    Norde, W.2
  • 3
    • 0029162070 scopus 로고
    • Understanding and increasing protein stability
    • C. O. Fagain 1995 Understanding and increasing protein stability Biochim. Biophys. Acta 1252 1 14
    • (1995) Biochim. Biophys. Acta , vol.1252 , pp. 1-14
    • Fagain, C.O.1
  • 4
    • 0028808838 scopus 로고
    • Relationships between molecular-states (conformation and orientation) and activities of alpha-amylase adsorbed on ultrafine silica particles
    • A. Kondo T. Urabe 1995 Relationships between molecular-states (conformation and orientation) and activities of alpha-amylase adsorbed on ultrafine silica particles Appl. Microbiol. Biotechnol. 43 801 807
    • (1995) Appl. Microbiol. Biotechnol. , vol.43 , pp. 801-807
    • Kondo, A.1    Urabe, T.2
  • 6
    • 10644244393 scopus 로고    scopus 로고
    • Micropipette manipulation: A technique to evaluate the stability of water-in-oil emulsions containing proteins
    • L. Jorgensen D. H. Kim C. Vermehren S. Bjerregaard S. Froekjaer 2004 Micropipette manipulation: a technique to evaluate the stability of water-in-oil emulsions containing proteins J. Pharm. Sci. 93 2994
    • (2004) J. Pharm. Sci. , vol.93 , pp. 2994
    • Jorgensen, L.1    Kim, D.H.2    Vermehren, C.3    Bjerregaard, S.4    Froekjaer, S.5
  • 7
    • 0030763365 scopus 로고    scopus 로고
    • Kinetic investigations by fluorescence correlation spectroscopy: The analytical and diagnostic potential of diffusion studies
    • P. Schwille J. Bieschke F. Oehlenschläger 1997 Kinetic investigations by fluorescence correlation spectroscopy: the analytical and diagnostic potential of diffusion studies Biophys. Chem. 66 211 228
    • (1997) Biophys. Chem. , vol.66 , pp. 211-228
    • Schwille, P.1    Bieschke, J.2    Oehlenschläger, F.3
  • 11
    • 0021244277 scopus 로고
    • Stabilisation of dissolved proteins against denaturation at hydrophobic interfaces
    • H. Thurow K. Geisen 1984 Stabilisation of dissolved proteins against denaturation at hydrophobic interfaces Diabetologia 27 212 218
    • (1984) Diabetologia , vol.27 , pp. 212-218
    • Thurow, H.1    Geisen, K.2
  • 12
    • 0026004620 scopus 로고
    • Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces
    • V. Sluzky J. A. Tamada A. M. Klibanov R. Langer 1991 Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces Proc. Natl. Acad. Sci. USA 88 9377 9381
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9377-9381
    • Sluzky, V.1    Tamada, J.A.2    Klibanov, A.M.3    Langer, R.4
  • 13
    • 0037453163 scopus 로고    scopus 로고
    • Secondary structure alterations in insulin and growth hormone water-in-oil emulsions
    • L. Jorgensen C. Vermehren S. Bjerregaard S. Froekjaer 2003 Secondary structure alterations in insulin and growth hormone water-in-oil emulsions Int. J. Pharm. 254 7 10
    • (2003) Int. J. Pharm. , vol.254 , pp. 7-10
    • Jorgensen, L.1    Vermehren, C.2    Bjerregaard, S.3    Froekjaer, S.4
  • 17
    • 0004103464 scopus 로고
    • Kluwer Academic Publishers Dordrecht
    • J. Brange 1994 Stability of Insulin Kluwer Academic Publishers Dordrecht
    • (1994) Stability of Insulin
    • Brange, J.1
  • 18
    • 77956751025 scopus 로고
    • Insulin: The structure in the crystal and its reflection in the chemistry and biology
    • T. Blundel D. Dodson D. Hodgkin D. Needham 1972 Insulin: the structure in the crystal and its reflection in the chemistry and biology Adv. Protein Chem. 26 279 402
    • (1972) Adv. Protein Chem. , vol.26 , pp. 279-402
    • Blundel, T.1    Dodson, D.2    Hodgkin, D.3    Needham, D.4
  • 20
    • 0019860250 scopus 로고
    • Self-association of insulin and the role of hydrophobic bonding: A thermodynamic model of insulin dimerization
    • Y. Pocker B. Biswas 1981 Self-association of insulin and the role of hydrophobic bonding: a thermodynamic model of insulin dimerization Biochemistry 20 4354 4361
    • (1981) Biochemistry , vol.20 , pp. 4354-4361
    • Pocker, Y.1    Biswas, B.2
  • 21
    • 0031573537 scopus 로고    scopus 로고
    • Synthesis and characterization of insulin fluorescein derivatives for bioanalytical applications
    • N. G. Hentz J. M. Richardson J. R. Sportsman G. S. Sittampalam 1997 Synthesis and characterization of insulin fluorescein derivatives for bioanalytical applications Anal. Chem. 69 4994 5000
    • (1997) Anal. Chem. , vol.69 , pp. 4994-5000
    • Hentz, N.G.1    Richardson, J.M.2    Sportsman, J.R.3    Sittampalam, G.S.4
  • 23
    • 2342614735 scopus 로고    scopus 로고
    • The LSM 510 META-ConfoCor 2 system: An integrated imaging and spectroscopic platform for single-molecule detection
    • K. Weisshart V. Jungel J. R. Clement 2004 The LSM 510 META-ConfoCor 2 system: an integrated imaging and spectroscopic platform for single-molecule detection Curr. Pharm. Biotechnol. 5 135 154
    • (2004) Curr. Pharm. Biotechnol. , vol.5 , pp. 135-154
    • Weisshart, K.1    Jungel, V.2    Clement, J.R.3
  • 24
    • 0023999464 scopus 로고
    • Photon correlation measurements at large lag times: Improving statistical accuracy
    • K. Schätzel M. Drewel S. Stimac 1988 Photon correlation measurements at large lag times: improving statistical accuracy J. Mod. Opt. 35 711 718
    • (1988) J. Mod. Opt. , vol.35 , pp. 711-718
    • Schätzel, K.1    Drewel, M.2    Stimac, S.3
  • 25
    • 0028229903 scopus 로고
    • Sorting single molecules: Application to diagnostics and evolutionary biotechnology
    • M. Eigen R. Rigler 1994 Sorting single molecules: application to diagnostics and evolutionary biotechnology Proc. Natl. Acad. Sci. 1994 5740
    • (1994) Proc. Natl. Acad. Sci. , vol.1994 , pp. 5740
    • Eigen, M.1    Rigler, R.2
  • 26
    • 0002830818 scopus 로고
    • Interactions and kinetics of single molecules as observed by fluorescence correlation spectroscopy
    • Springer Berlin
    • R. Rigler J. Widengren Ü Mets 1992 Interactions and kinetics of single molecules as observed by fluorescence correlation spectroscopy O. Wolfbeis Fluorescence Spectroscopy Springer Berlin 13 24
    • (1992) Fluorescence Spectroscopy , pp. 13-24
    • Rigler, R.1    Widengren, J.2    Mets U.̈3    Wolfbeis, O.4
  • 27
    • 0012936585 scopus 로고    scopus 로고
    • Theoretical study of detection of a dipole emitter through an objective with high numerical aperture
    • J. Enderlein 2000 Theoretical study of detection of a dipole emitter through an objective with high numerical aperture Opt. Lett. 25 634 636
    • (2000) Opt. Lett. , vol.25 , pp. 634-636
    • Enderlein, J.1
  • 28
    • 0000534243 scopus 로고
    • Ultrasensitive detection of single molecules as observed by fluorescence correlation spectroscopy
    • R. Rigler J. Widengren 1990 Ultrasensitive detection of single molecules as observed by fluorescence correlation spectroscopy BioScience 3 180 183
    • (1990) BioScience , vol.3 , pp. 180-183
    • Rigler, R.1    Widengren, J.2
  • 29
    • 32244444423 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy and its potential for intracellular applications
    • P. Schwille 2001 Fluorescence correlation spectroscopy and its potential for intracellular applications Cell Biochem. Biophys. 40 6036 6046
    • (2001) Cell Biochem. Biophys. , vol.40 , pp. 6036-6046
    • Schwille, P.1
  • 31
    • 0030511959 scopus 로고    scopus 로고
    • Mechanisms of photobleaching investigated by fluorescence correlation spectroscopy
    • J. Widengren R. Rigler 1996 Mechanisms of photobleaching investigated by fluorescence correlation spectroscopy Bioimaging 4 149 157
    • (1996) Bioimaging , vol.4 , pp. 149-157
    • Widengren, J.1    Rigler, R.2
  • 32
    • 13244298992 scopus 로고    scopus 로고
    • Reversible self-association of ovalbumin at air-water interfaces and the consequences for the exerted surface pressure
    • E. Kudryashova A. Visser H. Jongh 2005 Reversible self-association of ovalbumin at air-water interfaces and the consequences for the exerted surface pressure Protein Sci. 14 483 493
    • (2005) Protein Sci. , vol.14 , pp. 483-493
    • Kudryashova, E.1    Visser, A.2    Jongh, H.3
  • 33
    • 0033637148 scopus 로고    scopus 로고
    • Fluorescence intensity multiple distributions analysis: Concurrent determination of diffusion times and molecular brightness
    • K. Palo U. Mets S. Jager P. Kask K. Gall 2000 Fluorescence intensity multiple distributions analysis: concurrent determination of diffusion times and molecular brightness Biophys. J. 79 2858 2866
    • (2000) Biophys. J. , vol.79 , pp. 2858-2866
    • Palo, K.1    Mets, U.2    Jager, S.3    Kask, P.4    Gall, K.5
  • 34
    • 0032251894 scopus 로고    scopus 로고
    • Convergence properties of the Nelder-Mead simplex method in low dimensions
    • 1
    • J. Lagarias J. Reeds M. Wright P. Wright 1998 Convergence properties of the Nelder-Mead simplex method in low dimensions SIAM J. Optim. 9 1 112 147
    • (1998) SIAM J. Optim. , vol.9 , pp. 112-147
    • Lagarias, J.1    Reeds, J.2    Wright, M.3    Wright, P.4
  • 35
    • 0035010214 scopus 로고    scopus 로고
    • The standard deviation in fluorescence correlation spectroscopy
    • T. Wohland R. Rigler V. Vogel 2001 The standard deviation in fluorescence correlation spectroscopy Biophys. J. 80 2987 2999
    • (2001) Biophys. J. , vol.80 , pp. 2987-2999
    • Wohland, T.1    Rigler, R.2    Vogel, V.3
  • 36
    • 0000221607 scopus 로고    scopus 로고
    • The adsorption of proteins from aqueous solution on solid surfaces
    • M. Kleijn W. Norde 2004 The adsorption of proteins from aqueous solution on solid surfaces Heterog. Chem. Rev. 2 157 172
    • (2004) Heterog. Chem. Rev. , vol.2 , pp. 157-172
    • Kleijn, M.1    Norde, W.2
  • 37
    • 0032798799 scopus 로고    scopus 로고
    • Protein adsorption at the oil/water interface: Characterization of adsorption kinetics by dynamic interfacial tension measurements
    • C. J. Beverung C. J. Radke H. W. Blanch 1999 Protein adsorption at the oil/water interface: characterization of adsorption kinetics by dynamic interfacial tension measurements Biophys. Chem. 81 59 80
    • (1999) Biophys. Chem. , vol.81 , pp. 59-80
    • Beverung, C.J.1    Radke, C.J.2    Blanch, H.W.3
  • 39
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
    • L. Nielsen R. Khurana A. Coats S. Frokjaer J. Brange S. Vyas V. N. Uversky A. L. Fink 2001 Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism Biochemistry 40 6036 6046
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5    Vyas, S.6    Uversky, V.N.7    Fink, A.L.8
  • 40
    • 0037207098 scopus 로고    scopus 로고
    • Surface denaturation and amyloid fibril formation of insulin at model lipid-water interfaces
    • J. S. Sharp J. A. Forrest R. A. Jones 2002 Surface denaturation and amyloid fibril formation of insulin at model lipid-water interfaces Biochemistry 41 15810 15819
    • (2002) Biochemistry , vol.41 , pp. 15810-15819
    • Sharp, J.S.1    Forrest, J.A.2    Jones, R.A.3
  • 41


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.